Membrane Protein Topology Database

Welcome to MPtopo, a curated database of membrane proteins with experimentally validated transmembrane (TM) segments. If you publish work that used MPtopo, please cite Jayasinghe et al. (2001) Protein Sci. 10:455-458.

MPtopo has now been integrated with mpstruc. Unlike the previous version, MPtopo now includes only proteins of known 3D structure; the 1D_Helix entries, whose TM helices were identified by experimental techniques such as gene fusion, have been removed.

MPtopo Querier is no longer available as a separate application, but does remain integral to MPEx. The 'text search' below is similar to 'text search' in mpstruc. We will eventually add additional search capabilities found in the old MPtopo Querier. In addition, we will provide the same capabilities found on the mpstruc page, such as XML representations.

MPtopo currently contains a total of 165 proteins with 949 TM segments.

Latest new protein topology entered: 06 Feb 2007 at 16:00 PST.
Last MPtopo database update: 06 Jan 2022 at 16:01 PST

Summary of MPtopo Data*
Characteristic	Beta-Barrel TM Proteins	Alpha-Helical TM Proteins
*Not included in this table (but included in the database) are monotopic proteins and proteins with complex topologies, such as chloride channels, whose TM segments are not easily classified. A list of these proteins is available here (coming soon?).
Number of Proteins/Protein Subunits	25	119
Number of total residues	10294	27312
Number of residues in TM segments	4207	11848
Total number of TM segments	334	455
Average TM segment length	12±3	26±5
TM segment length range	6-23	10-48

Text Search of Table
Search Text: Limit 32 characters. Special characters in the search text should be explicitly represented. You can cut-and-paste them into the search string (the easiest approach), or they can be composed: e.g., on a mac, Å can be composed with keyboard shift-option-A. See this page for more examples.
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XML Representations
An XML representation provides a convenient machine or human-readable format of the portion of the data table that has been made visible, and allows you to build software tools to consume it as you see fit. You can use the URLs adjacent to the buttons below to access the same view the corresponding button provides.
	This button generates an XML representation of the currently visible portion of the table.
	https://blanco.biomol.uci.edu/mpstruc/mptopomptopoTblXml
	https://blanco.biomol.uci.edu/mpstruc/mptopomptopoMonotopicTblXml
	https://blanco.biomol.uci.edu/mpstruc/mptopomptopoBetaBrlTblXml
	https://blanco.biomol.uci.edu/mpstruc/mptopomptopoAlphaHlxTblXml
If your browser doesn’t directly display a nicely formatted XML page, it should provide a "view page source" menu selection that will. It should also provide a "save page" option so that you can download the XML formatted data. If you’re not familiar with XML and how to use it, a good source of information is available here. NOTES: Generated XML uses the following Document Type Definition (DTD): <!DOCTYPE mptopo [ <!ELEMENT mptopo (caption,groups)> <!ATTLIST mptopo createdBy CDATA #REQUIRED> <!ATTLIST mptopo maintainedBy CDATA #REQUIRED> <!ATTLIST mptopo copyright CDATA #REQUIRED> <!ATTLIST mptopo url CDATA #REQUIRED> <!ATTLIST mptopo lastNewMptopoProteinDate CDATA #REQUIRED> <!ATTLIST mptopo lastDatabaseEditDate CDATA #REQUIRED> <!ATTLIST mptopo timeStamp CDATA #REQUIRED> <!ELEMENT caption (#PCDATA)> <!ELEMENT groups (group)> <!ELEMENT group (name,mptopoProteins?,subgroups)> <!ELEMENT subgroups (subgroup)> <!ELEMENT subgroup (name,mptopoProteins)> <!ELEMENT name (#PCDATA)> <!ELEMENT mptopoProteins (mptopoProtein)> <!ELEMENT mptopoProtein (proteinName,species,taxonomicDomain,remarks,pirNumber, uniprotEntry,uniprotNumber,uniprotGene,uniprotName, pdbTitle,pdbCodes, nTerminal,sequence,complexTopology,tmSegments, bibliography,secondaryBibliographies)> <!ELEMENT proteinName (#PCDATA)> <!ELEMENT species (#PCDATA)> <!ELEMENT taxonomicDomain (#PCDATA)> <!ELEMENT remarks (#PCDATA)> <!ELEMENT pirNumber (#PCDATA)> <!ELEMENT uniprotEntry (#PCDATA)> <!ELEMENT uniprotNumber (#PCDATA)> <!ELEMENT uniprotGene (#PCDATA)> <!ELEMENT uniprotName (#PCDATA)> <!ELEMENT pdbTitle (#PCDATA)> <!ELEMENT pdbCodes (pdbCode)> <!ELEMENT pdbCode (#PCDATA)> <!ELEMENT nTerminal (#PCDATA)> <!ELEMENT sequence (#PCDATA)> <!ELEMENT complexTopology (#PCDATA)> <!ELEMENT tmSegments (tmSegment)> <!ELEMENT tmSegment (segLabel,beginIndex,endIndex)> <!ELEMENT segLabel (#PCDATA)> <!ELEMENT beginIndex (#PCDATA)> <!ELEMENT endIndex (#PCDATA)> <!ELEMENT bibliography (pubMedId,authors,year,title,journal,volume,issue,pages,doi,notes)> <!ELEMENT pubMedId (#PCDATA)> <!ELEMENT authors (#PCDATA)> <!ELEMENT year (#PCDATA)> <!ELEMENT title (#PCDATA)> <!ELEMENT journal (#PCDATA)> <!ELEMENT volume (#PCDATA)> <!ELEMENT issue (#PCDATA)> <!ELEMENT pages (#PCDATA)> <!ELEMENT doi (#PCDATA)> <!ELEMENT notes (#PCDATA)> <!ELEMENT secondaryBibliographies (bibliography*)> ]>

Membrane Protein Topology Database
Protein	UniProt ID	PDB ID	Reference (links are to PubMed)
MONOTOPIC MEMBRANE PROTEINS Reviewed by Allen et al. (2018) Database of Peripheral Membrane Proteins
Cyclooxygenases
*prostaglandin synthase-1 (COX-1) : Ovis aries (Sheep) E Eukaryota** *Monotopic membrane protein that binds on the membrane surface. 'tmsegs' denotes surface-binding helices. Protein is located in ER lumen. Sequence below is from Swiss-Prot. TMhelices=0. N Terminal: in TM Segment Count: 4 TM Segments: A.73,83; B.85,93; C.97,106; D.108,116; Sequence: MSRQSISLRFPLLLLLLSPSPVFSADPGAPAPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRTTLRPSPSFIHFMLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRILPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEHPTWGDEQLFQTARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDVIKESRVLRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLNTKTCPYVSFHVPDPRQEDRPGVERPPTEL	P05979 UniProt Entry: PGH1_SHEEP UniProt Gene: PTGS1, COX1 UniProt Name: Prostaglandin G/H synthase 1 [Precursor] PIR Number: S00561	1PRH PDB Title: prostaglandin H2 synthase-1 (cyclooxygenase I)	Picot et al. (1994). Picot D, Loll PJ, & Garavito RM (1994). The x-ray crystal structure of the membrane protein prostaglandin H₂synthase-1. Nature 367 :243-249. PubMed Id: 8121489.
*prostaglandin synthase-2 (COX-2) : Mus musculus E Eukaryota** *Monotopic membrane protein that binds to the membrane. 'tmsegs' denotes surface-binding helices. Protein is located in the ER lumen. Sequence is processed sequence from Swiss-Prot (17 AA signal sequence removed). TMhelices=0. N Terminal: in TM Segment Count: 4 TM Segments: A.75,82; B.89,95; C.97,105; D.109,113; Sequence: ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSLIMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLNHIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQVEMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHQRVCDILKQEHPEWGDEQLFQTSKLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLLPDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIAGRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFSLKPYTSFEELTGEKEMAAELKALYSDIDVMELYPALLVEKPRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFGGEVGFKIINTASIQSLICNNVKGCPFTSFNVQDPQPTKTATINASASHSRLDDINPTVLIKRRSTEL	Q05769 UniProt Entry: PGH2_MOUSE UniProt Gene: PTGS2, COX2, COX-2, TIS10, PGHS-B UniProt Name: Prostaglandin G/H synthase 2 [Precursor] PIR Number:	1CX2 PDB Title: cyclooxygenase-2, prostaglandin synthase-2	Kurumbail et al. (1996). Kurumbail RG, Stevens AM, Gierse JK, McDonald JJ, Stegeman RA, Pak JY, Gildehaus D, Miyashiro JM, Penning TD, Seibert, K et al (1996). Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents. Nature 384 :644-648. PubMed Id: 8967954.
Lipoxygenases Related to Cyclooxygenases Rather than being tethered by α-helices at the interface, they are tethered by N-terminal β-sheet C2-like domains
Squalene-Hopene Cyclases
*squalene-hopene cyclase : Alicyclobacillus acidocaldarius B Bacteria** *Monotopic membrane protein that binds to membrane surface. 'tmsegs' below indicates helices that interact with the membrane surface. Sequence is from PDB. It differs from Swiss-Prot by the addition Met1. TMhelices=0. N Terminal: in TM Segment Count: 1 TM Segments: A.216,231; Sequence: MAEQLVEAPAYARTLDRAVEYLLSCQKDEGYWWGPLLSNVTMEAEYVLLCHILDRVDRDRMEKIRRYLLHEQREDGTWALYPGGPPDLDTTIEAYVALKYIGMSRDEEPMQKALRFIQSQGGIESSRVFTRMWLALVGEYPWEKVPMVPPEIMFLGKRMPLNIYEFGSWARATVVALSIVMSRQPVFPLPERARVPELYETDVPPRRRGAKGGGGWIFDALDRALHGYQKLSVHPFRRAAEIRALDWLLERQAGDGSWGGIQPPWFYALIALKILDMTQHPAFIKGWEGLELYGVELDYGGWMFQASISPVWDTGLAVLALRAAGLPADHDRLVKAGEWLLDRQITVPGDWAVKRPNLKPGGFAFQFDNVYYPDVCDTAVVVWALNTLRLPDERRRRDAMTKGFRWIVGMQSSNGGWGAYDVDNTSDLPNHIPFSDFGEVTDPPSEDVTAHVLECFGSFGYDDAWKVIRRAVEYLKREQKPDGSWFGRWGVNYLYGTGAVVSALKAVGIDTREPYIQKALDWVEQHQNPDGGWGEDCRSYEDPAYAGKGASTPSQTAWALMALIAGGRAESEAARRGVQYLVETQRPDGGWDEPYYTGTGFPGDFYLGYTMYRHVFPTLALGRYKQAIERR	P33247 UniProt Entry: SQHC_ALIAC UniProt Gene: SHC UniProt Name: Squalene-hopene cyclase PIR Number: A43300, S13856	2SQC PDB Title: Squalene-Hopene Cyclase	Wendt et al. (1999). Wendt KU, Lenhart A, & Schulz GE (1999). The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution. J. Mol. Biol. 286 :175-187. PubMed Id: 9931258.
Oxidases
*Monoamine oxidase B : Homo sapiens E Eukaryota** Monotopic membrane protein because it binds to the membrane surface by a short helix anchor and surface interactions. Sequence is from PDB. It differs from Swiss-Prot by addition of Met1. TMhelices=0. N Terminal: out TM Segment Count: 1 TM Segments: A.489,515; Sequence: MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERLKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV	P27338 UniProt Entry: AOFB_HUMAN UniProt Gene: MAOB UniProt Name: Amine oxidase [flavin-containing] B PIR Number: B36175, JH0818	1GOS PDB Title: Human Monoamine Oxidase B	Binda et al. (2002). Binda C, Newton-Vinson P, Hubálek F, Edmondson DE, & Mattevi A (2002). Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nature Struct Biol 9 :22-26. PubMed Id: 11753429.
Hydrolases
*fatty acid amide hydrolase : Rattus norvegicus E Eukaryota** Monotopic membrane protein. Although this protein has a single transmembrane segment (tmseg A), it is classified as monotopic because the active site is external to the membrane. The binding of the protein to membranes is unaffected by removal of tmseg A. 'tmseg' B below refers to a helix-turn-helix motif that causes tight membrane association. Sequence is from Swiss-Prot. TMhelices=1. N Terminal: out TM Segment Count: 2 TM Segments: A.7,29; B.410,438; Sequence: MVLSEVWTTLSGVSGVCLACSLLSAAVVLRWTGRQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQLVQKLQSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAVPFVHTNVPQSMLSFDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSLGPMARDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGYYETDNYTMPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSAGGLFSDGGRSFLQNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAFLNSMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPALDLNTPGRATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFGDIWDIILKKAMKNSVGLPVAVQCVALPWQEELCLRFMREVEQLMTPQKQPS	P97612 UniProt Entry: FAAH_RAT UniProt Gene: FAAH UniProt Name: Fatty-acid amide hydrolase PIR Number:	1MT5 PDB Title: Fatty Acid Amide Hydrolase	Bracey et al. (2002). Bracey MH, Hanson MA, Masuda KR, Stevens RC, & Cravatt BF (2002). Structural adaptations in a membrane enzyme that terminates endo cannabinoid signaling. Science 298 :1793-1796. PubMed Id: 12459591.
Hydroxylases
Acyltransferases
Thioesterases
Nucleotidyltransferases
Oxidoreductases (Monotopic)
Dehydrogenases
Decarboxylases (Monotopic)
Glycosyltransferases
GPI-Anchored Cell-Wall Proteins (GPI-CWPs) GPIs are glycosylphophatidylinositol anchors that are post-translational modifications in eukaryotes
Phosphoglycosyl Transferases (PGT) These proteins catalyze the first membrane-committed step of glycoconjugates
Peptidases
Cytochromes P450 P450s are members of the CYP51 family involved in sterol biosynthesis
Dihydroorotate Dehydrogenases (DHODH, class 2) Class 1 DHODHs are soluble proteins. Class 2 are membrane associated proteins.
Polymerases
ADP-Ribosylation Factors
Isomerases
Phosphoinositide Kinases
Membrane-Shaping Proteins (monotopic)
Membrane Trafficking Proteins
Cell Adhesion Molecules
Guanosine Triphosphatases
Phospholipid Phosphatases
Sorting Nexins
Pro-apoptotic BCL-2 Family
Variant Surface Glycoproteins (VSG)
TRANSMEMBRANE PROTEINS: BETA-BARREL
Adventitious Membrane Proteins: Beta-sheet Pore-forming Toxins/Attack Complexes
*alpha-hemolysin: Staphylococcus aureus* B Bacteria** Heptameric beta-barrel toxin. Strands=2. Processed sequence from Swiss-Prot for monomer is shown (26 AA signal sequence removed), which is the same as sequence in PDB file. N Terminal: out TM Segment Count: 2 TM Segments: A.110,126; B.132,148; Sequence: ADSDINIKTGTTDIGSNTTVKTGDLVTYDKENGMHKKVFYSFIDDKNHNKKLLVIRTKGTIAGQYRVYSEEGANKSGLAWPSAFKVQLQLPDNEVAQISDYYPRNSIDTKEYMSTLTYGFNGNVTGDDTGKIGGLIGANVSIGHTLKYVQPDFKTILESPTDKKVGWKVIFNNMVNQNWGPYDRDSWNPVYGNQLFMKTRNGSMKAADNFLDPNKASSLLSSGFSPDFATVITMDRKASKQQTNIDVIYERVRDDYQLHWTSTNWKGTNTKDKWTDRSSERYKIDWEKEEMTN	P09616 UniProt Entry: HLA_STAAU UniProt Gene: HLY, HLA UniProt Name: Alpha-hemolysin [Precursor] PIR Number: S69209	7AHL PDB Title: alpha-hemolysin from Staphylococcus aureus	Song et al. (1996). Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, & Gouaux JE (1996). Structure of staphylococcal a -hemolysin, a heptameric transmembrane pore. Science 274 :1859-1866. PubMed Id: 8943190.
De novo Designed β-barrel Membrane Proteins β-barrel Proteins Designed from First Principles
Beta-Barrel Membrane Proteins: Porins and Relatives
*porin: Rhodobacter capsulatus* B Bacteria** Trimeric beta-barrel. Stands=16. Sequence from Swiss-Prot. N Terminal: in TM Segment Count: 16 TM Segments: A.1,15; B.18,35; C.39,47; D.59,65; E.68,74; F.118,125; G.127,135; H.148,158; I.160,171; J.181,192; K.194,206; L.227,240; M.242,255; N.258,271; O.274,285; P.292,301; Sequence: EVKLSGDARMGVMYNGDDWNFSSRSRVLFTMSGTTDSGLEFGASFKAHESVGAETGEDGTVFLSGAFGKIEMGDALGASEALFGDLYEVGYTDLDDRGGNDIPYLTGDERLTAEDNPVLLYTYSAGAFSVAASMSDGKVGETSEDDAQEMAVAAAYTFGNYTVGLGYEKIDSPDTALMADMEQLELAAIAKFGATNVKAYYADGELDRDFARAVFDLTPVAAAATAVDHKAYGLSVDSTFGATTVGGYVQVLDIDTIDDVTYYGLGASYDLGGGASIVGGIADNDLPNSDMVADLGVKFKF	P31243 UniProt Entry: PORI_RHOCA UniProt Gene: UniProt Name: porin PIR Number: S16070	2POR PDB Title: porin (crystal form B)	Weiss & Schulz (1992). Weiss MS & Schulz GE (1992). Structure of porin refined at 1.8 Å resolution. J. Mol. Biol. 227 :493-509. PubMed Id: 1328651.
*outer membrane porin: Rhodopseudomonas blastica* B Bacteria** Trimeric beta-barrel. Strands=16. Sequence from Swiss-Prot. N Terminal: in TM Segment Count: 16 TM Segments: A.1,16; B.24,41; C.45,57; D.69,75; E.77,84; F.131,139; G.141,150; H.163,172; I.174,183; J.193,201; K.205,214; L.222,232; M.234,245; N.252,261; O.264,274; P.278,289; Sequence: EISLNGYGRFGLQYVEDRGVGLEDTIISSRLRINIVGTTETDQGVTFGAKLRMQWDDGDAFAGTAGNAAQFWTSYNGVTVSVGNVDTAFDSVALTYDSEMGYEASSFGDAQSSFFAYNSKYDASGALDNYNGIAVTYSISGVNLYLSYVDPDQTVDSSLVTEEFGIAADWSNDMISLAAAYTTDAGGIVDNDIAFVGAAYKFNDAGTVGLNWYDNGLSTAGDQVTLYGNYAFGATTVRAYVSDIDRAGADTAYGIGADYQFAEGVKVSGSVQSGFANETVADVGVRFDF	P39767 UniProt Entry: PORI_RHOBL UniProt Gene: OPMA UniProt Name: Porin PIR Number: S38806	1PRN PDB Title: porin	Kreusch & Schulz (1994). Kreusch A & Schulz GE (1994). Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus. J Mol Biol 243 :891-905. PubMed Id: 7525973. doi:10.1006/jmbi.1994.1690.
*OmpK36 osmoporin : Klebsiella pneumoniae B Bacteria** The first (A) and 17th (A) 'tmsegs' abut to form a single strand. Trimeric beta-barrel. Strands=16. Sequence is processed sequence from Swiss-Prot (21 AA signal sequence removed). N Terminal: in TM Segment Count: 17 TM Segments: A.1,6; B.9,23; C.36,50; D.56,66; E.79,89; F.94,99; G.135,142; H.151,158; I.173,181; J.185,195; K.210,221; L.225,235; M.253,263; N.270,279; O.290,302; P.307,316; *A.330,340; Sequence: AEIYNKDGNKLDLYGKIDGLHYFSDDKDVDGDQTYMRLGVKGETQINDQLTGYGQWEYNVQANNTESSSDQAWTRLAFAGLKFGDAGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFLQSRANGVATYRNSDFFGLVDGLNFALQYQGKNGSVSGEGATNNGRGALKQNGDGFGTSVTYDIFDGISAGFAYANSKRTDDQNQLLLGEGDHAETYTGGLKYDANNIYLATQYTQTYNATRAGSLGFANKAQNFEVAAQYQFDFGLRPSVAYLQSKGKDLNGYGDQDILKYVDVGATYYFNKNMSTYVDYKINLLDDNSFTRSAGISTDDVVALGLVYQF	Q48473 UniProt Entry: OMPC_KLEPN UniProt Gene: OMPC, OMPK36 UniProt Name: Outer membrane protein C [Precursor] PIR Number:	1OSM PDB Title: Ompk36	Dutzler et al. (1999). Dutzler R, Rummel G, Alberti S, Hernandez-Alles S, Phale P, Rosenbusch J, Benedi V, & Schirmer T (1999). Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae. Structure Fold. Des 7 :425-434. PubMed Id: 10196126.
*Omp32: Comamonas acidovorans* B Bacteria** Trimeric beta-barrel. Strands=16. Periplasm = in. Sequence from Swiss-Prot is processed form (19 AA signal sequence removed). N Terminal: in TM Segment Count: 16 TM Segments: A.3,17; B.26,47; C.52,61; D.77,83; E.86,95; F.133,142; G.148,156; H.170,180; I.183,196; J.199,214; K.218,231; L.235,249; M.253,265; N.269,282; O.286,300; P.320,332; Sequence: QSSVTLFGIVDTNVAYVNKDAAGDSRYGLGTSGASTSRLGLRGTEDLGGGLKAGFWLEGEIFGDDGNASGFNFKRRSTVSLSGNFGEVRLGRDLVPTSQKLTSYDLFSATGIGPFMGFRNWAAGQGADDNGIRANNLISYYTPNFGGFNAGFGYAFDEKQTIGTADSVGRYIGGYVAYDNGPLSASLGLAQQKTAVGGLATDRDEITLGASYNFGVAKLSGLLQQTKFKRDIGGDIKTNSYMLGASAPVGGVGEVKLQYALYDQKAIDSKAHQITLGYVHNLSKRTALYGNLAFLKNKDASTLGLQAKGVYAGGVQAGESQTGVQVGIRHAF	P24305 UniProt Entry: OM32_COMAC UniProt Gene: OMP32 UniProt Name: Outer membrane porin protein 32 [Precursor] PIR Number: A38528	1E54 PDB Title: ANION-SELECTIVE PORIN FROM COMAMONAS ACIDOVORANS	Zeth et al. (2000). Zeth K, Diederichs K, Welte W, & Engelhardt H (2000). Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 A resolution. Structure 8 :981-992. PubMed Id: 10986465.
*OmpF porin : Escherichia coli B Bacteria** TM seg. A (1-6) joins with C-terminus of TM seg. A (331-340) to form a complete segment. Trimeric beta-barrel. Strands=16. Nterm in = periplasm. Sequence shown is the processed sequence from Swiss-Prot, which is the same as the sequence in the PDB file. Topology & strand assignments are virtually identical to PhoE. N Terminal: in TM Segment Count: 17 TM Segments: A.1,6; B.8,23; C.38,51; D.54,65; E.83,91; F.94,100; G.135,141; H.150,161; I.170,182; J.184,195; K.211,222; L.224,235; M.253,265; N.268,281; O.292,303; P.306,315; *A.331,340; Sequence: AEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGATYYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF	P02931 UniProt Entry: OMPF_ECOLI UniProt Gene: OMPF, TOLF, CMLB, COA, CRY, B0929 UniProt Name: Outer membrane protein F [Precursor] PIR Number: MMECF	1OPF PDB Title: matrix porin (OmpF)	Cowan et al. (1992). Cowan SW, Schirmer T, Rummel G, Steiert M, Ghosh R, Pauptit RA, Jansonius JN, & Rosenbusch JP (1992). Crystal structures explain functional properties of two Escherichia coli porins. Nature 358 :727-733. PubMed Id: 1380671.
*PhoE phosphoporin : Escherichia coli B Bacteria** Trimeric beta-barrel. Nterm in = periplasm. Strands=16. Sequence shown is the processed sequence from Swiss-Prot, which is the same as the sequence in the PDB file. TM seg. A* (1-6) joins with C-terminus of TM seg. A (324-330) to form a complete segment. Topology & strand assignments are virtually identical to OmpF. N Terminal: in TM Segment Count: 17 TM Segments: A.1,6; B.8,23; C.34,47; D.50,61; E.78,86; F.89,95; G.131,137; H.146,157; I.166,178; J.182,193; K.209,220; L.222,233; M.246,258; N.261,274; O.285,296; P.299,308; *A.324,330; Sequence: AEIYNKDGNKLDVYGKVKAMHYMSDNASKDGDQSYIRFGFKGETQINDQLTGYGRWEAEFAGNKAESDTAQQKTRLAFAGLKYKDLGSFDYGRNLGALYDVEAWTDMFPEFGGDSSAQTDNFMTKRASGLATYRNTDFFGVIDGLNLTLQYQGKNENRDVKKQNGDGFGTSLTYDFGGSDFAISGAYTNSDRTNEQNLQSRGTGKRAEAWATGLKYDANNIYLATFYSETRKMTPITGGFANKTQNFEAVAQYQFDFGLRPSLGYVLSKGKDIEGIGDEDLVNYIDVGATYYFNKNMSAFVDYKINQLDSDNKLNINNDDIVAVGMTYQF	P02932 UniProt Entry: PHOE_ECOLI UniProt Gene: PHOE, OMPE, B0241 UniProt Name: Outer membrane pore protein E [Precursor] PIR Number: MMECPE	1PHO PDB Title: phosphoporin (Phoe)	Cowan et al. (1992). Cowan SW, Schirmer T, Rummel G, Steiert M, Ghosh R, Pauptit RA, Jansonius JN, & Rosenbusch JP (1992). Crystal structures explain functional properties of two Escherichia coli porins. Nature 358 :727-733. PubMed Id: 1380671.
*maltoporin: Salmonella typhimurium* B Bacteria** Trimeric beta-barrel. Strands=18. Nterm in = periplasm. Sequence shown is the processed sequence from Swiss-Prot (25 AA signal sequence removed), which is the same as the sequence in the PDB file. N Terminal: in TM Segment Count: 18 TM Segments: A.2,15; B.40,53; C.56,68; D.80,90; E.98,105; F.124,134; G.137,148; H.167,180; I.185,197; J.210,223; K.226,238; L.276,290; M.293,308; N.312,326; O.329,344; P.348,363; Q.371,385; R.412,427; Sequence: VDFHGYARSGIGWTGSGGEQQCFQATGAQSKYRLGNECETYAELKLGQEVWKEGDKSFYFDTNVAYSVNQQNDWESTDPAFREANVQGKNLIEWLPGSTIWAGKRFYQRHDVHMIDFYYWDISGPGAGIENIDLGFGKLSLAATRSTEAGGSYTFSSQNIYDEVKDTANDVFDVRLAGLQTNPDGVLELGVDYGRANTTDGYKLADGASKDGWMFTAEHTQSMLKGYNKFVVQYATDAMTTQGKGQARGSDGSSSFTEELSDGTKINYANKVINNNGNMWRILDHGAISLGDKWDLMYVGMYQNIDWDNNLGTEWWTVGVRPMYKWTPIMSTLLEVGYDNVKSQQTGDRNNQYKITLAQQWQAGDSIWSRPAIRIFATYAKWDEKWGYIKDGDNISRYAAASNSGISTNSRGDSDEWTFGAQMEIWW	P26466 UniProt Entry: LAMB_SALTY UniProt Gene: LAMB, MALL, STM4231 UniProt Name: Maltoporin [Precursor] PIR Number: A60177	2MPR PDB Title: maltoporin from Salmonella typhimurium	Meyer et al. (1997). Meyer JEW, Hofnung M, & Schulz GE (1997). Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J. Mol. Biol 266 :761-775. PubMed Id: 9102468.
*maltoporin: Escherichia coli* B Bacteria** Trimeric beta-barrel. Strands=18. Nterm in = periplasm. Sequence shown is processed sequence from Swiss-Prot (25 AA signal sequence removed), which is the same as sequence in PDB file. Related RM# 13837. N Terminal: in TM Segment Count: 18 TM Segments: A.2,14; B.40,53; C.56,68; D.80,89; E.99,105; F.124,132; G.138,148; H.167,179; I.186,196; J.211,223; K.226,238; L.267,280; M.284,296; N.303,316; O.320,333; P.339,352; Q.362,373; R.408,421; Sequence: VDFHGYARSGIGWTGSGGEQQCFQTTGAQSKYRLGNECETYAELKLGQEVWKEGDKSFYFDTNVAYSVAQQNDWEATDPAFREANVQGKNLIEWLPGSTIWAGKRFYQRHDVHMIDFYYWDISGPGAGLENIDVGFGKLSLAATRSSEAGGSSSFASNNIYDYTNETANDVFDVRLAQMEINPGGTLELGVDYGRANLRDNYRLVDGASKDGWLFTAEHTQSVLKGFNKFVVQYATDSMTSQGKGLSQGSGVAFDNEKFAYNINNNGHMLRILDHGAISMGDNWDMMYVGMYQDINWDNDNGTKWWTVGIRPMYKWTPIMSTVMEIGYDNVESQRTGDKNNQYKITLAQQWQAGDSIWSRPAIRVFATYAKWDEKWGYDYTGNADNNANFGKAVPADFNGGSFGRGDSDEWTFGAQMEIWW	P02943 UniProt Entry: LAMB_ECOLI UniProt Gene: LAMB, MALB, B4036 UniProt Name: Maltoporin [Precursor] PIR Number: QRECL	1MAL PDB Title: maltoporin	Schirmer et al. (1995). Schirmer T, Keller TA, Wang YF, & Rosenbusch JP (1995). Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267 :512-4. PubMed Id: 7824948.
*porin scrY, sucrose-specific: Salmonella typhimurium* B Bacteria** Trimeric beta-barrel. Strands=18. Sequence from Swiss-Prot with leader sequence (22 AA) removed. Periplasm = in. N Terminal: in TM Segment Count: 18 TM Segments: A.73,82; B.117,128; C.134,145; D.159,168; E.181,188; F.206,213; G.222,233; H.241,253; I.256,264; J.286,296; K.306,316; L.335,344; M.351,363; N.371,384; O.389,403; P.413,426; Q.439,449; R.472,482; Sequence: QTDISTIEARLNALEKRLQEAENRAQTAENRAGAAEKKVQQLTAQQQKNQNSTQEVAQRTARLEKKADDKSGFEFHGYARSGVIMNDSGASTKSGAYITPAGETGGAIGRLGNQADTYVEMNLEHKQTLDNGATTRFKVMVADGQTSYNDWTASTSDLNVRQAFVELGNLPTFAGPFKGSTLWAGKRFDRDNFDIHWIDSDVVFLAGTGGGIYDVKWNDGLRSNFSLYGRNFGDIDDSSNSVQNYILTMNHFAGPLQMMVSGLRAKDNDERKDSNGNLAKGDAANTGVHALLGLHNDSFYGLRDGSSKTALLYGHGLGAEVKGIGSDGALRPGADTWRIASYGTTPLSENWSVAPAMLAQRSKDRYADGDSYQWATFNLRLIQAINQNFALAYEGSYQYMDLKPEGYNDRQAVNGSFYKLTFAPTFKVGSIGDFFSRPEIRFYTSWMDWSKKLNNYASDDALGSDGFNSGGEWSFGVQMETWF	P22340 UniProt Entry: SCRY_SALTY UniProt Gene: SCRY UniProt Name: Sucrose porin [Precursor] PIR Number: S15193	1A0S 1A0T PDB Title: sucrose-specific porin, with bound sucrose molecules	Forst et al. (1998). Forst D, Welte W, Wacker T, & Diederichs K (1998). Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nature Structural Biol 5 :37-46. PubMed Id: 9437428.
*MspA: Mycobacterium smegmatis* B Bacteria** Homooctameric beta-barrel porin. Strands=16 for octamer. TMsegs below are for a monomer. in=periplasm. Sequence is from TrEMBL. The 27AA presequence has been removed. N Terminal: out TM Segment Count: 2 TM Segments: A.72,90; B.104,121; Sequence: GLDNELSLVDGQDRTLTVQQWDTFLNGVFPLDRNRLTREWFHSGRAKYIVAGPGADEFEGTLELGYQIGFPWSLGVGINFSYTTPNILIDDGDITAPPFGLNSVITPNLFPGVSISADLGNGPGIQEVATFSVDVSGAEGGVAVSNAHGTVTGAAGGVLLRPFARLIASTGDSVTTYGEPWNMN	Q9RLP7 UniProt Entry: Q9RLP7_MYCSM UniProt Gene: mspA UniProt Name: mSPa [precursor] PIR Number:	1UUN PDB Title: MspA	Faller et al. (2004). Faller M, Niederweis M, & Schulz GE (2004). The structure of a mycobacterial outer-membrane channel. Science 303 :1189-1192. PubMed Id: 14976314.
*OprP: Pseudomonas aeruginosa* B Bacteria** 16-stranded beta-barrel. Trimeric form. Sequence for monomer from PDB file. Sequence in Swiss-Prot has additional 29 aa at the beginning as a signal sequence. There is no signal sequence in PDB file. Thus res#1 in PDB file corresponds to res#30 in Swiss-Prot file. N Terminal: in TM Segment Count: 16 TM Segments: A.28,42; B.53,69; C.73,80; D.93,100; E.107,112; F.148,156; G.161,170; H.181,194; I.197,209; J.255,269; K.272,285; L.292,304; M.331,345; N.360,372; O.377,389; P.399,410; Sequence: GTVTTDGADIVIKTKGGLEVATTDKEFSFKLGGRLQADYGRFDGYYTNNGNTADAAYFRRAYLEFGGTAYRDWKYQINYDLSRNVGNDSAGYFDEASVTYTGFNPVNLKFGRFYTDFGLEKATSSKWVTALERNLTYDIADWVNDNVGTGIQASSVVGGMAFLSGSVFSENNNDTDGDSVKRYNLRGVFAPLHEPGNVVHLGLQYAYRDLEDSAVDTRIRPRMGMRGVSTNGGNDAGSNGNRGLFGGSSAVEGLWKDDSVWGLEGAWALGAFSAQAEYLRRTVKAERDREDLKASGYYAQLAYTLTGEPRLYKLDGAKFDTIKPENKEIGAWELFYRYDSIKVEDDNIVVDSATREVGDAKGKTHTLGVNWYANEAVKVSANYVKAKTDKISNANGDDSGDGLVMRLQYVF	P05695 UniProt Entry: PORP_PSEAE UniProt Gene: oprP UniProt Name: Porin P [Precursor] PIR Number:	2O4V PDB Title: An arginine ladder in OprP mediates phosphate specific transfer across the outer membrane	Moraes et al. (2007). Moraes TF, Bains M, Hancock REW & Strynadka NCJ (2007). An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane. Nature Struc Mol Biol 14 :85-87. PubMed Id: 17187075.
Outer Membrane Carboxylate Channels (Occ) These outer membrane proteins require substrates to have a carboxyl group for efficient transport. OccD channels are selective for basic amino acids. OccK channels prefer cyclic substrates. See Eren et al. (2012).
Beta-Barrel Membrane Proteins: Monomeric/Dimeric
*outer membrane protein TolC : Escherichia coli B Bacteria** *Trimeric beta-barrel transmembrane domain. Strands=4. Sequence and strands shown for one monomer. Sequence below is the processed sequence from Swiss-Prot (22 AA signal sequence removed). N Terminal: in TM Segment Count: 4 TM Segments: A.41,52; B.61,74; C.247,257; D.279,289; Sequence: ENLMQVYQQARLSNPELRKSAADRDAAFEKINEARSPLLPQLGLGADYTYSNGYRDANGINSNATSASLQLTQSIFDMSKWRALTLQEKAAGIQDVTYQTDQQTLILNTATAYFNVLNAIDVLSYTQAQKEAIYRQLDQTTQRFNVGLVAITDVQNARAQYDTVLANEVTARNNLDNAVEQLRQITGNYYPELAALNVENFKTDKPQPVNALLKEAEKRNLSLLQARLSQDLAREQIRQAQDGHLPTLDLTASTGISDTSYSGSKTRGAAGTQYDDSNMGQNKVGLSFSLPIYQGGMVNSQVKQAQYNFVGASEQLESAHRSVVQTVRSSFNNINASISSINAYKQAVVSAQSSLDAMEAGYSVGTRTIVDVLDATTTLYNAKQELANARYNYLINQLNIKSALGTLNEQDLLALNNALSKPVSTNPENVAPQTPEQNAIADGYAPDSPAPVVQQTSARTTTSNGHNPFRN	P02930 UniProt Entry: TOLC_ECOLI UniProt Gene: TOLC, MTCB, MUKA, REFI, B3035 UniProt Name: Outer membrane protein tolC [Precursor] PIR Number: MMECTC	1EK9 PDB Title: Outer Membrane Protein Tolc, Chain A, B, C	Koronakis et al. (2000). Koronakis V, Sharff A, Koronakis E, Luisi B, & Hughes C (2000). Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405 :914-919. PubMed Id: 10879525.
*vitamin B12 receptor: Escherichia coli* B Bacteria** Monomeric beta barrel. Strands=22. Sequence is from Swiss-Prot. The leader sequence (residues 1-20) has been removed in sequence below to correspond to sequence in PDB. N Terminal: in TM Segment Count: 22 TM Segments: A.137,145; B.149,159; C.164,175; D.197,209; E.214,227; F.243,257; G.261,276; H.289,305; I.309,322; J.334,348; K.351,362; L.366,380; M.383,394; N.413,426; O.429,447; P.452,472; Q.475,488; R.501,510; S.515,523; T.544,554; U.559,566; V.585,594; Sequence: QDTSPDTLVVTANRFEQPRSTVLAPTTVVTRQDIDRWQSTSVNDVLRRLPGVDITQNGGSGQLSSIFIRGTNASHVLVLIDGVRLNLAGVSGSADLSQFPIALVQRVEYIRGPRSAVYGSDAIGGVVNIITTRDEPGTEISAGWGSNSYQNYDVSTQQQLGDKTRVTLLGDYAHTHGYDVVAYGNTGTQAQTDNDGFLSKTLYGALEHNFTDAWSGFVRGYGYDNRTNYDAYYSPGSPLLDTRKLYSQSWDAGLRYNGELIKSQLITSYSHSKDYNYDPHYGRYDSSATLDEMKQYTVQWANNVIVGHGSIGAGVDWQKQTTTPGTGYVEDGYDQRNTGIYLTGLQQVGDFTFEGAARSDDNSQFGRHGTWQTSAGWEFIEGYRFIASYGTSYKAPNLGQLYGFYGNPNLDPEKSKQWEGAFEGLTAGVNWRISGYRNDVSDLIDYDDHTLKYYNEGKARIKGVEATANFDTGPLTHTVSYDYVDARNAITDTPLLRRAKQQVKYQLDWQLYDFDWGITYQYLGTRYDKDYSSYPYQTVKMGGVSLWDLAVAYPVTSHLTVRGKIANLFDKDYETVYGYQTAGREYTLSGSYTF	P06129 UniProt Entry: BTUB_ECOLI UniProt Gene: btuB UniProt Name: Vitamin B12 receptor, Precursor PIR Number: QRECBT	1NQE PDB Title: Vitamin B12 Receptor	Chimento et al. (2003). Chimento DP, Mohanty AK, Kadner RJ, & Wiener MC (2003). Substrate-induced transmembrane signaling in the cobalamin transporter BtuB. Nat Struct Biol. 10 :394-401. PubMed Id: 12652322.
*OmpA: Escherichia coli* B Bacteria** Monomeric beta-barrel. Strands=8. Sequence is processed sequence from Swiss-Prot (21 AA signal sequence removed). N Terminal: in TM Segment Count: 8 TM Segments: A.6,16; B.34,45; C.49,60; D.75,86; E.91,103; F.121,130; G.135,143; H.161,170; Sequence: APKDNTWYTGAKLGWSQYHDTGFINNNGPTHENQLGAGAFGGYQVNPYVGFEMGYDWLGRMPYKGSVENGAYKAQGVQLTAKLGYPITDDLDIYTRLGGMVWRADTKSNVYGKNHDTGVSPVFAGGVEYAITPEIATRLEYQWTNNIGDAHTIGTRPDNGMLSLGVSYRFGQGEAAPVVAPAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGMGESNPVTGNTCDNVKQRAALIDCLAPDRRVEIEVKGIKDVVTQPQA	P0A910 UniProt Entry: OMPA_ECOLI UniProt Gene: OMPA, TOLG, TUT, CON, B0957, Z1307, ECS1041 UniProt Name: Outer membrane protein A [Precursor] PIR Number: A90759, G85622	1BXW 1QJP 1G90 PDB Title: Outer Membrane Protein A (Ompa)	Pautsch & Schulz (1998). Pautsch A & Schulz GE (1998). Structure of the outer membrane protein A transmembrane domain. Nature Struct Biol 5 :1013-1017. PubMed Id: 9808047.
*OmpT: Escherichia coli* B Bacteria** Monomeric beta-barrel protein. Strands=10. Sequence below is processed sequence from Swiss-Prot (20 AA signal sequence removed). Periplasm = in. N Terminal: in TM Segment Count: 10 TM Segments: A.10,21; B.49,61; C.64,73; D.109,119; E.126,137; F.177,189; G.192,203; H.230,241; I.244,255; J.285,297; Sequence: STETLSFTPDNINADISLGTLSGKTKERVYLAEEGGRKVSQLDWKFNNAAIIKGAINWDLMPQISIGAAGWTTLGSRGGNMVDQDWMDSSNPGTWTDESRHPDTQLNYANEFDLNIKGWLLNEPNYRLGLMAGYQESRYSFTARGGSYIYSSEEGFRDDIGSFPNGERAIGYKQRFKMPYIGLTGSYRYEDFELGGTFKYSGWVESSDNDEHYDPGKRITYRSKVKDQNYYSVAVNAGYYVTPNAKVYVEGAWNRVTNKKGNTSLYDHNNNTSDYSKNGAGIENYNFITTAGLKYTF	P09169 UniProt Entry: OMPT_ECOLI UniProt Gene: OMPT, B0565 UniProt Name: Protease VII [Precursor] PIR Number: A31387	1I78 PDB Title: Crystal Structure Of Outer Membrane Protease Ompt From Escherichia Coli	Vandeputte-Rutten et al. (2001). Vandeputte-Rutten L, Kramer RA, Kroon J, Dekker N, Egmond, MR, & Gros P (2001). Crystal structure of the outer membrane protease OmpT from Eschericia coli suggests a novel catalytic site. EMBO J 20 :5033-5039. PubMed Id: 11566868.
*OmpW: Escherichia coli* B Bacteria** Monomeric 8-stranded beta-barrel. Sequence from PDB. Sequence in Swiss-Prot has additional 21 aa at the beginning as a signal sequence. There is no signal sequence in PDB file and that is why res#1 in PDB file corresponds to res#22 in Swiss-Prot file N Terminal: in TM Segment Count: 8 TM Segments: A.6,16; B.36,48; C.51,67; D.71,89; E.96,114; F.131,141; G.148,164; H.174,191; Sequence: HEAGEFFMRAGSATVRPTEGAGGTLGSLGGFSVTNNTQLGLTFTYMATDNIGVELLAATPFRHKIGTRATGDIATVHHLPPTLMAQWYFGDASSKFRPYVGAGINYTTFFDNGFNDHGKEAGLSDLSLKDSWGAAGQVGVDYLINRDWLVNMSVWYMDIDTTANYKLGGAQQHDSVRLDPWVFMFSAGYRF	P0A915 UniProt Entry: OMPW_ECOLI UniProt Gene: ompW UniProt Name: Outer membrane protein W [Precursor] PIR Number: S07797, T45501	2F1T 2F1V PDB Title: Outer membrane protein OmpW	Hong et al. (2006). Hong H, Patel DR, Tamm LK, & van den Berg B (2006). The Outer Membrane Protein OmpW Forms an Eight-stranded beta-Barrel with a Hydrophobic Channel. J Biol Chem 281 :7568-7577. PubMed Id: 16414958.
*OmpX: Escherichia coli* B Bacteria** monomeric beta-barrel. Strands=8. Sequence is processed sequence from Swiss-Prot (23 AA signal sequence removed). N Terminal: in TM Segment Count: 8 TM Segments: A.2,13; B.20,32; C.36,47; D.62,72; E.76,87; F.107,117; G.120,131; H.137,147; Sequence: ATSTVTGGYAQSDAQGQMNKMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRTASSGDYNKNQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKHDTSDYGFSYGAGLQFNPMENVALDFSYEQSRIRSVDVGTWIAGVGYRF	P0A917 UniProt Entry: OMPX_ECOLI UniProt Gene: OMPX, B0814, C0900, Z1036, ECS0892, SF0765, S0807 UniProt Name: Outer membrane protein X [Precursor] PIR Number:	1QJ9 PDB Title: Outer Membrane Protein X	Vogt & Schulz (1999). Vogt J & Schulz GE (1999). The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence. Structure Fold.Des. 7 :1301-1309. PubMed Id: 10545325.
*outer membrane phospholipase A: Escherichia coli* B Bacteria** Monomeric/Dimeric beta-barrel. Strands=12. Nterm in = periplasm. Sequence is processed Swiss-Prot sequence (20 AA signal sequence removed). N Terminal: in TM Segment Count: 12 TM Segments: A.33,45; B.65,79; C.86,98; D.109,128; E.131,144; F.154,166; G.169,178; H.193,203; I.206,214; J.221,230; K.236,245; L.255,264; Sequence: QEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYDTNYLIYTQTSDLNKEAIASYDWAENARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVGNTDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNWNTGYGGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF	P0A921 UniProt Entry: PA1_ECOLI UniProt Gene: PLDA, B3821, Z5342, ECS4751, SF3899 UniProt Name: Phospholipase A1 [Precursor] PIR Number: PSECA1	1QD5 1QD6 PDB Title: Outer Membrane Phospholipase A; Chain	Snijder et al. (1999). Snijder HJ, Ubarretxena-Belandia I, Blaauw M, Kalk KH, Verheij HM, Egmond MR, Dekker N, & Dijkstra BW (1999). Structural evidence for dimerization-regulated activation of an integral membrane phospholipase. Nature 401 :717-721. PubMed Id: 10537112.
*OpcA: Neisseria meningitidis* B Bacteria** Monomeric beta-barrel. Strands=10. Processed sequence from TrEMBL (19 AA signal sequence removed). N Terminal: in TM Segment Count: 10 TM Segments: A.8,18; B.34,44; C.49,58; D.88,99; E.107,118; F.135,147; G.153,164; H.188,199; I.205,215; J.244,253; Sequence: AQELQTANEFTVHTDLSSISSTRAFLKEKHKAAKHIGVRADIPFDANQGIRLEAGFGRSKKNIINLETDENKLGKTKNVKLPTGVPENRIDLYTGYTYTQTLSDSLNFRVGAGLGFESSKDSIKTTKHTLHSSRQSWLAKVHADLLSQLGNGWYINPWSEVKFDLNSRYKLNTGVTNLKKDINQKTNGWGFGLGANIGKKLGESASIEAGPFYKQRTYKESGEFSVTTKSGDVSLTIPKTSIREYGLRVGIKF		1K24 PDB Title: Opca Outer Membrane Adhesin/Invasin	Prince et al. (2002). Prince SM, Achtman M, & Derrick JP (2002). Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis. Proc. Natl. Acad. Sci. USA 99 :3417-3421. PubMed Id: 11891340.
*NspA surface protein A: Neisseria meningitidis* B Bacteria** Monomeric beta-barrel. Sequence is processed sequence from Swiss-Prot (19 AA signal sequence removed). Strands=8. N Terminal: in TM Segment Count: 8 TM Segments: A.5,17; B.26,37; C.40,51; D.60,74; E.78,90; F.105,118; G.122,130; H.140,155; Sequence: EGASGFYVQADAAHAKASSSLGSAKGFSPRISAGYRINDLRFAVDYTRYKNYKAPSTDFKLYSIGASAIYDFDTQSPVKPYLGARLSLNRASVDLGGSDSFSQTSIGLGVLTGVSYAVTPNVDLDAGYRYNYIGKVNTVKNVRSGELSVGVRVKF	P96943 UniProt Entry: P96943_NEIME UniProt Gene: nspA UniProt Name: Outer membrane protein [Precursor] PIR Number:	1P4T PDB Title: Outer Membrane Protein Nspa	Vandeputte-Rutten et al. (2003). Vandeputte-Rutten L, Bos MP, Tommassen J, & Gros P (2003). Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential. J. Biol. Chem. 278 :24825-24830. PubMed Id: 12716881.
*PagP: Escherichia coli* B Bacteria** Monomeric beta barrel. Strands=8. PDB sequence truncated by 25 residues. TM segments numbered according to Swiss-Prot CrcA sequence. To get PDB numbering, subtract 25 from CrcA numbering. N Terminal: in TM Segment Count: 8 TM Segments: A.47,57; B.76,86; C.90,100; D.106,118; E.127,138; F.146,158; G.161,169; H.177,186; Sequence: MNVSKYVAIFSFVFIQLISVGKVFANADEWMTTFRENIAQTWQQPEHYDLYIPAITWHARFAYDKEKTDRYNERPWGGGFGLSRWDEKGNWHGLYAMAFKDSWNKWEPIAGYGWESTWRPLADENFHLGLGFTAGVTARDNWNYIPLPVLLPLASVGYGPVTFQMTYIPGTYNNGNVYFAWMRFQF	P37001 UniProt Entry: CRCA_ECOLI UniProt Gene: CRCA, B0622 UniProt Name: CrcA protein PIR Number:	1MM4 PDB Title: Crca protein	Hwang et al. (2002). Hwang PM, Choy WY, Lo EI, Chen L, Forman-Kay JD, Raetz CR, Privé GG, Bishop RE, Kay LE (2002). Solution structure and dynamics of the outer membrane enzyme PagP by NMR. Proc Natl Acad Sci USA 99 :13560-13565. PubMed Id: 12357033.
*FadL: Escherichia coli* B Bacteria** Monomeric, 14-stranded beta-barrel. N terminus in hatch domain. Sequence from PDB. Sequence in Swiss-Prot file has additional 25 aa at the beginning as a signal sequence. Sequence in PDB doesn't have a signal sequence so res#1 in PDB file corresponds to res#26 in Swiss-Prot file. N Terminal: out TM Segment Count: 14 TM Segments: A.44,60; B.76,87; C.92,107; D.120,134; E.140,156; F.199,218; G.221,240; H.263,284; I.287,308; J.313,333; K.339,348; L.366,376; M.381,399; N.402,420; Sequence: AGFQLNEFSSSGLGRAYSGEGAIADDAGNVSRNPALITMFDRPTFSAGAVYIDPDVNISGTSPSGRSLKADNIAPTAWVPNMHFVAPINDQFGWGASITSNYGLATEFNDTYAGGSVGGTTDLETMNLNLSGAYRLNNAWSFGLGFNAVYARAKIERFAGDLGQLVAGQIMQSPAGQTQQGQALAATANGIDSNTKIAHLNGNQWGFGWNAGILYELDKNNRYALTYRSEVKIDFKGNYSSDLNRAFNNYGLPIPTATGGATQSGYLTLNLPEMWEVSGYNRVDPQWAIHYSLAYTSWSQFQQLKATSTSGDTLFQKHEGFKDAYRIALGTTYYYDDNWTFRTGIAFDDSPVPAQNRSISIPDQDRFWLSAGTTYAFNKDASVDVGVSYMHGQSVKINEGPYQFESEGKAWLFGTNFNYAF	P10384 UniProt Entry: FADL_ECOLI UniProt Gene: fadL UniProt Name: Long-chain fatty acid transport protein [Precursor] PIR Number: F65007	1T16 1T1L PDB Title: Crystal structure of the bacterial fatty acid transporter FadL from Escherichia coli	van den Berg et al. (2004). van den Berg B, Black PN, Clemons WM Jr, & Rapoport TA (2004). Crystal structure of the long-chain fatty acid transporter FadL. Science 304 :1506-1509. PubMed Id: 15178802.
*Ferric hydroxamate uptake receptor: Escherichia coli* B Bacteria** Monomeric beta-barrel. Strands=22. Sequence is processed sequence from Swiss-Prot (33 AA signal sequence removed). N Terminal: in TM Segment Count: 22 TM Segments: A.160,168; B.174,182; C.190,198; D.213,221; E.227,235; F.280,288; G.294,302; H.355,363; I.371,380; J.432,441; K.444,453; L.476,485; M.489,497; N.520,528; O.533,541; P.569,578; Q.581,589; R.613,622; S.628,637; T.658,666; U.672,680; V.706,714; Sequence: AVEPKEDTITVTAAPAPQESAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSVLYGKSSPGGLLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDFSDSLDDDGVYSYRLTGLARSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPETGYYGWLPKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNLRFAENKTSQNSVYGYGVCSDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQNFSVDTQLQSKFATGDIDHTLLTGVDFMRMRNDINAWFGYDDSVPLLNLYNPSHHHHHHGSVNTDFDFNAKDPANSGPYRILNKQKQTGVYVQDQAQWDKVLVTLGGRYDWADQESLNRVAGTTDKRDDKQFTWRGGVNYLFDNGVTPYFSYSESFEPSSQVGKDGNIFAPSKGKQYEVGVKYVPEDRPIVVTGAVYNLTKTNNLMADPEGSFFSVEGGEIRARGVEIEAKAALSASVNVVGSYTYTDAEYTTDTTYKGNTPAQVPKHMASLWADYTFFDGPLSGLTLGTGGRYTGSSYGDPANSFKVGSYTVVDALVRYDLARVGMAGSNVALHVNNLFDREYVASCFNTYGCFWGAERQVVATATFRF	P06971 UniProt Entry: FHUA_ECOLI UniProt Gene: FHUA, TONA, B0150 UniProt Name: Ferrichrome-iron receptor [Precursor] PIR Number:	2FCP PDB Title: ferric hydroxamate uptake receptor	Ferguson et al. (1998). Ferguson AD, Hofmann E, Coulton JW, Diederichs K, & Welte W (1998). Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Protein Sci 9 :956-963. PubMed Id: 9856937.
*FepA: Escherichia coli* B Bacteria** Monomeric beta-barrel. Strands=22. Sequence is processed sequence from Swiss-Prot (22 AA signal sequence removed). N Terminal: in TM Segment Count: 22 TM Segments: A.154,164; B.172,182; C.187,197; D.229,241; E.245,255; F.283,293; G.302,313; H.343,356; I.360,371; J.408,419; K.424,434; L.441,451; M.456,467; N.505,517; O.521,532; P.560,574; Q.578,589; R.605,616; S.619,628; T.654,664; U.669,679; V.716,723; Sequence: QEPTDTPVSHDDTIVVTAAEQNLQAPGVSTITADEIRKNPVARDVSKIIRTMPGVNLTGNSTSGQRGNNRQIDIRGMGPENTLILIDGKPVSSRNSVRQGWRGERDTRGDTSWVPPEMIERIEVLRGPAAARYGNGAAGGVVNIITKKGSGEWHGSWDAYFNAPEHKEEGATKRTNFSLTGPLGDEFSFRLYGNLDKTQADAWDINQGHQSARAGTYATTLPAGREGVINKDINGVVRWDFAPLQSLELEAGYSRQGNLYAGDTQNTNSDSYTRSKYGDETNRLYRQNYALTWNGGWDNGVTTSNWVQYEHTRNSRIPEGLAGGTEGKFNEKATQDFVDIDLDDVMLHSEVNLPIDFLVNQTLTLGTEWNQQRMKDLSSNTQALTGTNTGGAIDGVSTTDRSPYSKAEIFSLFAENNMELTDSTIVTPGLRFDHHSIVGNNWSPALNISQGLGDDFTLKMGIARAYKAPSLYQTNPNYILYSKGQGCYASAGGCYLQGNDDLKAETSINKEIGLEFKRDGWLAGVTWFRNDYRNKIEAGYVAVGQNAVGTDLYQWDNVPKAVVEGLEGSLNVPVSETVMWTNNITYMLKSENKTTGDRLSIIPEYTLNSTLSWQAREDLSMQTTFTWYGKQQPKKYNYKGQPAVGPETKEISPYSIVGLSATWDVTKNVSLTGGVDNLFDKRLWRAGNAQTTGDLAGANYIAGAGAYTYNEPGRTWYMSVNTHF	P05825 UniProt Entry: FEPA_ECOLI UniProt Gene: FEPA, FEP, FEUB, B0584 UniProt Name: Ferrienterobactin receptor [Precursor] PIR Number: QRECFC	1FEP PDB Title: Ferric Enterobactin Receptor	Buchanan et al. (1999). Buchanan S, Smith BS, Venkatramani L, Xia D, Esser L, Palnitkar M, Chakraborty R, van der Helm D, & Deisenhofer J. (1999). Crystal Structure of the outer membrane active transporter FepA from Escherichia coli. Nature Structural Biol 6 :56-63. PubMed Id: 9886293.
*FecA: Escherichia coli* B Bacteria** Monomeric beta-barrel. Strands=22. Sequence is the processed sequence from Swiss-Prot (33 AA signal sequence removed). N Terminal: in TM Segment Count: 22 TM Segments: A.223,235; B.242,254; C.258,269; D.279,289; E.296,305; F.338,346; G.352,362; H.382,393; I.402,413; J.447,456; K.460,470; L.488,499; M.505,515; N.536,546; O.551,562; P.582,592; Q.604,614; R.634,643; S.647,657; T.681,692; U.698,709; V.732,741; Sequence: AQVNIAPGSLDKALNQYAAHSGFTLSVDASLTRGKQSNGLHGDYDVESGLQQLLDGSGLQVKPLGNNSWTLEPAPAPKEDALTVVGDWLGDARENDVFEHAGARDVIRREDFAKTGATTMREVLNRIPGVSAPENNGTGSHDLAMNFGIRGLNPRLASRSTVLMDGIPVPFAPYGQPQLSLAPVSLGNMDAIDVVRGGGAVRYGPQSVGGVVNFVTRAIPQDFGIEAGVEGQLSPTSSQNNPKETHNLMVGGTADNGFGTALLYSGTRGSDWREHSATRIDDLMLKSKYAPDEVHTFNSLLQYYDGEADMPGGLSRADYDADRWQSTRPYDRFWGRRKLASLGYQFQPDSQHKFNIQGFYTQTLRSGYLEQGKRITLSPRNYWVRGIEPRYSQIFMIGPSAHEVGVGYRYLNESTHEMRYYTATSSGQLPSGSSPYDRDTRSGTEAHAWYLDDKIDIGNWTITPGMRFEHIESYQNNAITGTHEEVSYNAPLPALNVLYHLTDSWNLYANTEGSFGTVQYSQIGKAVQSGNVEPEKARTWELGTRYDDGALTAEMGLFLINFNNQYDSNQTNDTVTARGKTRHTGLETQARYDLGTLTPTLDNVSIYASYAYVNAEIREKGDTYGNLVPFSPKHKGTLGVDYKPGNWTFNLNSDFQSSQFADNANTVKESADGSTGRIPGFMLWGARVAYDFGPQMADLNLAFGVKNIFDQDYFIRSYDDNNKGIYAGQPRTLYMQGSLKF	P13036 UniProt Entry: FECA_ECOLI UniProt Gene: FECA, B4291 UniProt Name: Iron(III) dicitrate transport protein fecA [Precursor] PIR Number: QRECFA	1KMO 1KMP PDB Title: Iron(III) Dicitrate Transport Protein Feca	Ferguson et al. (2002). Ferguson AD, Chakraborty R, Smith BS, Esser L, van der Helm D, & Deisenhofer, J (2002). Structural basis of gating by the outer Membrane transporter FecA. Science 295 :1715-1719. PubMed Id: 11872840.
*FptA: Pseudomonas aeruginosa* B Bacteria** 22-stranded beta-barrel. Sequence from Swiss-Prot. N Terminal: in TM Segment Count: 22 TM Segments: A.187,196; B.200,210; C.217,230; D.236,248; E.254,268; F.298,312; G.317,334; H.355,376; I.378,400; J.423,445; K.451,466; L.469,485; M.491,502; N.517,531; O.536,548; P.570,584; Q.589,602; R.621,631; S.638,654; T.657,674; U.679,686; V.710,720; Sequence: MKTETKVIKGRQGIARNRHTPLCLGLLLALSPLAAAVADARKDGETELPDMVISGESTSATQPPGVTTLGKVPLKPRELPQSASVIDHERLEQQNLFSLDEAMQQATGVTVQPFQLLTTAYYVRGFKVDSFELDGVPALLGNTASSPQDMAIYERVEILRGSNGLLHGTGNPAATVNLVRKRPQREFAASTTLSAGRWDRYRAEVDVGGPLSASGNVRGRAVAAYEDRDYFYDVADQGTRLLYGVTEFDLSPDTLLTVGAQYQHIDSITNMAGVPMAKDGSNLGLSRDTYLDVDWDRFKWDTYRAFGSLEQQLGGGWKGKVSAEYQEADSRLRYAGSFGAIDPQTGDGGQLMGAAYKFKSIQRSLDANLNGPVRLFGLTHELLGGVTYAQGETRQDTARFLNLPNTPVNVYRWDPHGVPRPQIGQYTSPGTTTTTQKGLYALGRIKLAEPLTLVVGGRESWWDQDTPATRFKPGRQFTPYGGLIWDFARDWSWYVSYAEVYQPQADRQTWNSEPLSPVEGKTYETGIKGELADGRLNLSLAAFRIDLENNPQEDPDHPGPPNNPFYISGGKVRSQGFELEGTGYLTPYWSLSAGYTYTSTEYLKDSQNDSGTRYSTFTPRHLLRLWSNYDLPWQDRRWSVGGGLQAQSDYSVDYRGVSMRQGGYALVNMRLGYKIDEHWTAAVNVNNLFDRTYYQSLSNPNWNNRYGEPRSFNVSLRGAF	P42512 UniProt Entry: FPTA_PSEAE UniProt Gene: fptA UniProt Name: Fe(3+)-pyochelin receptor [Precursor] PIR Number: A36942	1XKW PDB Title: Pyochelin outer membrane receptor FptA from Pseudomonas aeruginosa	Cobessi et al. (2005). Cobessi D, Celia H, Pattus F (2005). Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa. J Mol Biol 352 :893-904. PubMed Id: 16139844.
Outer Membrane Autotransporters
*NaIP translocator domain: Neisseria meningitidis* B Bacteria** Monomeric beta-barrel. strands=12. in=periplasm. There is also an alpha-helix but it is buried inside the beta-barrel. Sequence is from PDB file. Sequence is truncated relative to Swiss-Prot and starts at res#777. N Terminal: out TM Segment Count: 12 TM Segments: A.42,57; B.60,78; C.81,96; D.98,116; E.120,138; F.144,162; G.171,188; H.198,220; I.223,234; J.264,277; K.280,291; L.294,307; Sequence: DGVRIFNSLAATVYADSTAAHADMQGRRLKAVSDGLDHNGTGLRVIAQTQQDGGTWEQGGVEGKMRGSTQTVGIAAKTGENTTAAATLGMGRSTWSENSANAKTDSISLFAGIRHDAGDIGYLKGLFSYGRYKNSISRSTGADEHAEGSVNGTLMQLGALGGVNVPFAATGDLTVEGGLRYDLLKQDAFAEKGSALGWSGNSLTEGTLVGLAGLKLSQPLSDKAVLFATAGVERDLNGRDYTVTGGFTGATAATGKTGARNMPHTRLVAGLGADVEFGNGWNGLARYSYAGSKQYGNHSGRVGVGYRF	Q8GKS5 UniProt Entry: Q8GKS5_NEIME UniProt Gene: naIP UniProt Name: NaIP PIR Number:	1UYN 1UYO PDB Title: TRANSLOCATOR DOMAIN OF AUTOTRANSPORTER NALP FROM NEISSERIA MENINGITIDIS	Oomen et al. (2004). Oomen CJ, Van Ulsen P, Van Gelder P, Feijen M, Tommassen J, & Gros P (2004). Structure of the translocator domain of a bacterial autotransporter. EMBO J 23 :1257-1266. PubMed Id: 15014442.
*Hia autotransporter: Haemophilus influenzae* B Bacteria** Homotrimer. Monomer is a 4-stranded beta-barrel with one alpha-helix. The homotrimer thus has 3 alpha-helices burried inside a 12-stranded beta-barrel. Sequence for monomer from Swiss-Prot. N Terminal: out TM Segment Count: 4 TM Segments: A.1044,1055; B.1058,1068; C.1074,1084; D.1087,1096; Sequence: MNKIFNVIWNVVTQTWVVVSELTRTHTKCASATVAVAVLATLLSATVEANNNTPVTNKLKAYGDANFNFTNNSIADAEKQVQEAYKGLLNLNEKNASDKLLVEDNTAATVGNLRKLGWVLSSKNGTRNEKSQQVKHADEVLFEGKGGVQVTSTSENGKHTITFALAKDLGVKTATVSDTLTIGGGAAAGATTTPKVNVTSTTDGLKFAKDAAGANGDTTVHLNGIGSTLTDTLVGSPATHIDGGDQSTHYTRAASIKDVLNAGWNIKGVKAGSTTGQSENVDFVHTYDTVEFLSADTETTTVTVDSKENGKRTEVKIGAKTSVIKEKDGKLFTGKANKETNKVDGANATEDADEGKGLVTAKDVIDAVNKTGWRIKTTDANGQNGDFATVASGTNVTFASGNGTTATVTNGTDGITVKYDAKVGDGLKLDGDKIAADTTALTVNDGKNANNPKGKVADVASTDEKKLVTAKGLVTALNSLSWTTTAAEADGGTLDGNASEQEVKAGDKVTFKAGKNLKVKQEGANFTYSLQDALTGLTSITLGTGNNGAKTEINKDGLTITPANGAGANNANTISVTKDGISAGGQSVKNVVSGLKKFGDANFDPLTSSADNLTKQNDDAYKGLTNLDEKGTDKQTPVVADNTAATVGDLRGLGWVISADKTTGGSTEYHDQVRNANEVKFKSGNGINVSGKTVNGRREITFELAKGEVVKSNEFTVKETNGKETSLVKVGDKYYSKEDIDLTTGQPKLKDGNTVAAKYQDKGGKVVSVTDNTEATITNKGSGYVTGNQVADAIAKSGFELGLADEADAKAAFDDKTKALSAGTTEIVNAHDKVRFANGLNTKVSAATVESTDANGDKVTTTFVKTDVELPLTQIYNTDANGKKITKVVKDGQTKWYELNADGTADMTKEVTLGNVDSDGKKVVKDNDGKWYHAKADGTADKTKGEVSNDKVSTDEKHVVSLDPNDQSKGKGVVIDNVANGDISATSTDAINGSQLYAVAKGVTNLAGQVNNLEGKVNKVGKRADAGTASALAASQLPQATMPGKSMVAIAGSSYQGQNGLAIGVSRISDNGKVIIRLSGTTNSQGKTGVAAGVGYQW	Q48152 UniProt Entry: Q48152_HAEIN UniProt Gene: hia UniProt Name: Hia PIR Number:	2GR8 2GR7 PDB Title: Hia 1022-1098, Hia 992-1098	Meng et al. (2006). Meng G, Surana NK, St Geme JW 3rd, Waksman G (2006). Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter. EMBO J 25 :2297-2304. PubMed Id: 16688217.
Omp85-TpsB Outer Membrane Transporter Superfamily
Mitochondrial Outer Membrane Beta Barrel Proteins
Lipopolysaccharide (LPS) Transport Proteins
Polysaccharide Utilization Proteins Genes of this family are part of the starch utilization system (SUS)
Type II Secretion Systems
Type III Secretion Systems
Type IV Secretion Systems
Type VI Secretion Systems
Type IX Secretion Systems
Forespore Sporulation Channels These are ring-shaped conduits that connect the mother cell and forespore during sporulation.
Gasdermin (GSDM) Family Gasdermins are multi-subunit β-barrel forming proteins The gasdermins are expressed in the skin, mucosa, and immune antigen-presenting cells.
TRANSMEMBRANE PROTEINS: ALPHA-HELICAL
Adventitious Membrane Proteins: Alpha-helical Pore-forming Toxins.
De novo Designed Membrane Proteins Functional Proteins Designed from First Principles
*phospholamban pentamer: Homo sapiens* E Eukaryota** Sequence from PDB. Sequence is for one monomer in pentamer. Also see 1FJK, 1FJP (cardiac phospholamban from pig) N Terminal: in TM Segment Count: 1 TM Segments: A.23,52; Sequence: MEKVQYLTRSAIRRASTIEMPQQARQKLQNLFINFCLILICLLLICIIVMLL	PPLA_HUMAN UniProt Entry: P26678 UniProt Gene: PLN UniProt Name: Cardiac phospholamban PIR Number: A40424	1ZLL PDB Title: NMR Structure of Unphosphorylated Human Phospholamban Pentamer	Oxenoid and Chou (2005). Oxenoid K & Chou JJ (2005). The structure of phospholamban pentamer reveals a channel-like architecture in membranes. Proc Natl Acad Sci USA 102 :10870-10875. PubMed Id: 16043693.
Novel Membrane Proteins Membrane proteins that are not readily classified
Mammalian Cell Entry (MCE) Proteins These protein are involved in lipid trafficking between inner and outer bacterial membranes. The name originates from the erroneous early belief that they mediate mammalian cell entry in M. tuberculosis
Outer Membrane Proteins
Bacterial Cell Divison Proteins These proteins comprise the so-called 'divisome'
Chemotaxis Protein Complexes
Autoinducer Export Superfamily Proteins in this family are involved in cell-to-cell comminications, such as quorum sensing (QS)
Tetraspanins Mediate essential functions in the immune, reproductive, genitourinary, and auditory systems
Membrane-Spanning 4-Domain (MS4) Family
Autonomously Folding "Membrane Proteins" (Sec-independent)
Virus Coat Proteins
*M13 coat protein: Enterobacteria phage m13* V Viruses** S-P differs from PDB sequence at two residue positions. Sequence from PDB. TMhelices=1. N Terminal: out TM Segment Count: 1 TM Segments: A.24,45; Sequence: AEGDDPAKAAFNSLQASATEYIGYAWAMVVVIVGATIGIKLFKKFTSKAS	P03618 UniProt Entry: COAB_BPZJ2 UniProt Gene: VIII UniProt Name: Coat protein B PIR Number:	2CPB 2CPS PDB Title: M13 major coat protein	Papavoine et al. (1998). Papavoine CH, Christiaans BE, Folmer RH, Konings RN, & Hilbers CW (1998). Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues. J Mol Biol 282 :401-419. PubMed Id: 9735296. doi:10.1006/jmbi.1998.1860.
Glycoproteins
*glycophorin A: Homo sapiens* E Eukaryota** Sequence is processed sequence from Swiss-Prot (19 AA signal sequence removed). TMhelices=1. N Terminal: out TM Segment Count: 1 TM Segments: A.73,95; Sequence: SSTTGVAMHTSTSSSVTKSYISSQTNDTHKRDTYAATPRAHEVSEISVRTVYPPEEETGERVQLAHHFSEPEITLIIFGVMAGVIGTILLISYGIRRLIKKSPSDVKPLPSPDTDVPLSSVEIENPETSDQ	P02724 UniProt Entry: GLPA_HUMAN UniProt Gene: GYPA, GPA UniProt Name: Glycophorin A [Precursor] PIR Number: GFHUE	1AFO PDB Title: Glycophorin A, Chain A	MacKenzie et al. (1997). MacKenzie KR, Prestegard JH, & Engelman DM (1997). A transmembrane helix dimer: structure and implications. Science 276 :131-133. PubMed Id: 9082985.
High-Density Lipoprotein (HDL) Receptors
Tumor Necrosis Factor (TNF) Receptor Superfamily
B Cell Receptor Complexes These complexes are involved B cell development and immune responses
Receptor Tyrosine Kinase (RTK) Family Single-span TM proteins important in cellular signalling
Epidermal Growth Factor Receptors (EGFRs) ErbB (or HER) family of receptor tyrosine kinases (RTKs)
Erythropoietin-Producing Hepatocellular Receptors Eph family of receptor tyrosine kinases (RTKs)
Fibroblast Growth Factor Receptors FGFR family of receptor tyrosine kinases (RTKs)
Vascular Endothelial Growth Factor Receptors VEGFR family of receptor tyrosine kinases (RTKs)
Integrin Adhesion Receptors
Adiponectin Receptors 7TM receptors with inverted topology relative to GPCR receptors Adiponectin is a protein hormone that is important in glucose & fatty acid metabolism
Cytokine Receptors
Toll-Like Receptors (TLR) and TLR Signalling Regulators
Novel Receptors
Bacterial, Algal, Viral, and Unusual Rhodopsins
*bacteriorhodopsin: Halobacterium salinarium* A Archaea** Sequence below is processed sequence from Swiss-Prot (13 AA signal sequence removed). TMhelices=7. N Terminal: out TM Segment Count: 7 TM Segments: A.9,31; B.36,63; C.81,101; D.104,127; E.133,155; F.164,192; G.200,225; Sequence: QAQITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARYADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESMRPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAEAPEPSAGDGAAATSD	P02945 UniProt Entry: BACR_HALSA UniProt Gene: bop UniProt Name: Bacteriorhodopsin [Precursor] PIR Number: RAHSB	1BRX 2BRD 1AP9 1AT9 PDB Title: bacteriorhodopsin	Luecke et al. (1999). Luecke H, Schobert B, Richter HT, Cartailler P, & Lanyi JK (1999). Structure of bacteriorhodopsin at 1.55 angstrom resolution. J. Mol. Biol 291 :899-911. PubMed Id: 10452895.
*halorhodopsin: Halobacterium salinarum* A Archaea** Sequence below is unprocessed sequence from Swiss-Prot. AA numbering in PDB file and in the 'tmseg' assignments correspond to unprocessed sequence. Signal sequence corresponds to first 21 AA. TMhelices=7. N Terminal: out TM Segment Count: 7 TM Segments: A.26,51; B.58,81; C.106,127; D.131,154; E.158,180; F.193,216; G.227,255; Sequence: MSITSVPGVVDAGVLGAQSAAAVRENALLSSSLWVNVALAGIAILVFVYMGRTIRPGRPRLIWGATLMIPLVSISSYLGLLSGLTVGMIEMPAGHALAGEMVRSQWGRYLTWALSTPMILLALGLLADVDLGSLFTVIAADIGMCVTGLAAAMTTSALLFRWAFYAISCAFFVVVLSALVTDWAASASSAGTAEIFDTLRVLTVVLWLGYPIVWAVGVEGLALVQSVGVTSWAYSVLDVFAKYVFAFILLRWVANNERTVAVAGQTLGTMSSDD	P16102 UniProt Entry: BACH_HALSA UniProt Gene: HOP, VNG0180G UniProt Name: Halorhodopsin [Precursor] PIR Number: A26161	1E12 PDB Title: Halorhodopsin - Chain A	Kolbe et al. (2000). Kolbe M, Besir H, Essen L-O, & Oesterhelt D (2000). Structure of the light-driven chloride pump halorhodopsin at 1.8 Å. Science 288 :1390-1396. PubMed Id: 10827943.
*sensory rhodopsin: Anabaena* B Bacteria** Sequence from PDB N Terminal: out TM Segment Count: 7 TM Segments: A.3,26; B.34,56; C.72,91; D.99,121; E.125,147; F.159,185; G.195,209; Sequence: MNLESLLHWIYVAGMTIGALHFWSLSRNPRGVPQYEYLVAMFIPIWSGLAYMAMAIDQGKVEAAGQIAHYARYIDWMVTTPLLLLSLSWTAMQFIKKDWTLIGFLMSTQIVVITSGLIADLSERDWVRYLWYICGVCAFLIILWGIWNPLRAKTRTQSSELANLYDKLVTYFTVLWIGYPIVWIIGPSGFGWINQTIDTFLFCLLPFFSKVGFSFLDLHGLRNLNDSRQTTGDRFAENTLQFVENITLFANSRRQQSRRRV	Q8YSC4 UniProt Entry: Q8YSC4_ANASP UniProt Gene: alr3165 UniProt Name: bacteriorhodopsin PIR Number: AF2201	1XIO PDB Title: Anabaena sensory rhodopsin	Vogeley et al. (2004). Vogeley L, Sineshchekov OA, Trivedi VD, Sasaki J, Spudich JL, & Luecke H (2004). Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 Å. Science 306 :1390-1393. PubMed Id: 15459346.
*sensory rhodopsin II: Natronomonas pharaonis* A Archaea** Sequence is from Swiss-Prot. TMhelices=7. N Terminal: out TM Segment Count: 7 TM Segments: A.3,26; B.33,56; C.70,92; D.94,118; E.122,150; F.153,181; G.189,219; Sequence: MVGLTTLFWLGAIGMLVGTLAFAWAGRDAGSGERRYYVTLVGISGIAAVAYVVMALGVGWVPVAERTVFAPRYIDWILTTPLIVYFLGLLAGLDSREFGIVITLNTVVMLAGFAGAMVPGIERYALFGMGAVAFLGLVYYLVGPMTESASQRSSGIKSLYVRLRNLTVILWAIYPFIWLLGPPGVALLTPTVDVALIVYLDLVTKVGFGFIALDAAATLRAEHGESLAGVDTDAPAVAD	P42196 UniProt Entry: BACT_NATPH UniProt Gene: SOP2, SOPII UniProt Name: Sensory rhodopsin II PIR Number: S55300	1H68 1JGJ PDB Title: Sensory Rhodopsin II	Royant et al. (2001). Royant A, Nollert P, Edman K, Neutze R, Landau EM, & Pebay-Peyroula E. (2001). X-ray structure of sensory rhodopsin II at 2.1 Å resolution. Proc Natl Acad Sci USA 98 :10131-10136. PubMed Id: 11504917.
*sensory rhodopsin transducer: Natronomonas pharaonis* A Archaea** Sequence from Swiss-Prot. PDB sequence is truncated at N- & C-terminii. TMhelices=2. N Terminal: in TM Segment Count: 2 TM Segments: A.24,49; B.54,80; Sequence: MSLNVSRLLLPSRVRHSYTGKMGAVFIFVGALTVLFGAIAYGEVTAAAATGDAAAVQEAAVSAILGLIILLGINLGLVAATLGGDTAASLSTLAAKASRMGDGDLDVELETRREDEIGDLYAAFDEMRQSVRTSLEDAKNAREDAEQAQKRAEEINTELQAEAERFGEVMDRCADGDFTQRLDAETDNEAMQSIEGSFNEMMDGIEALVGRIERFADAVSEDAEAVRANAESVMEASEDVNRAVQNISDAAGDQTETVQQIALEMDDVSATTEEVAASADDIAKTARQAAETGEAGRETAETAITEMNEVESRTEQAVASMEELNEDVREIGEVSEMIADIAEQTNILALNASIEAARADGNSEGFAVVADEVKALAEETKAATEEIDDLIGTVQDRTQTTVDDIRETSDQVSEGVETVEDTVDALERIVDSVERTNDGIQEINQSTDAQADAAQKATTMVEDMAATSEQTASDAETAAETTETQAESVKEVFDLIDGLSEQADSLSETLSRTDTEEASAADLDDQPTLAAGDD	P42259 UniProt Entry: HTR2_NATPH UniProt Gene: HTR2, HTRII UniProt Name: Sensory rhodopsin II transducer PIR Number: S55299	1H2S PDB Title: rhodopsin II-transducer complex	Gordeliy et al. (2002). Gordeliy VI, Labahn J, Moukhametzianov R, Efremov R, Granzin J, Schlesinger R, Büldt G, Savopol T, Scheidig AJ, Klare JP, & Engelhard M. (2002). Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex. Nature 419 :484-487. PubMed Id: 12368857.
Adenylyl Cyclases Membrane-integral adenylyl cyclases are important enzymes in G protein-dependent signal transduction
Histidine Kinase Receptors
Immune Receptors
SNARE Protein Family
Claudins Claudins form the backbone of tight junctions
TMEM16 Family Proteins A functionally diverse family of proteins also known as Anoctamins
XKR Family of Proteins Kell blood group precursor proteins, often involved apoptotic lipid scrambling
Sec, Translocase, and Insertase Proteins Membrane Proteins Involved with Protein Secretion and Insertion formerly listed as "Channels: Protein-Conducting"
*SecY complex, alpha subunit: Methanococcus jannaschii* A Archaea** SecY protein. Cytoplasm = in. Sequence is from Swiss-Prot with Met1 removed so that it corresponds to the sequence in the PDB file. TMhelices=10. N Terminal: in TM Segment Count: 10 TM Segments: A.22,45; B.74,90; C.101,129; D.137,164; E.169,202; F.207,229; G.254,276; H.313,333; I.364,396; J.400,425; Sequence: KKLIPILEKIPEVELPVKEITFKEKLKWTGIVLVLYFIMGCIDVYTAGAQIPAIFEFWQTITASRIGTLITLGIGPIVTAGIIMQLLVGSGIIQMDLSIPENRALFQGCQKLLSIIMCFVEAVLFVGAGAFGILTPLLAFLVIIQIAFGSIILIYLDEIVSKYGIGSGIGLFIAAGVSQTIFVGALGPEGYLWKFLNSLIQGVPNIEYIAPIIGTIIVFLMVVYAECMRVEIPLAHGRIKGAVGKYPIKFVYVSNIPVILAAALFANIQLWGLALYRMGIPILGHYEGGRAVDGIAYYLSTPYGLSSVISDPIHAIVYMIAMIITCVMFGIFWVETTGLDPKSMAKRIGSLGMAIKGFRKSEKAIEHRLKRYIPPLTVMSSAFVGFLATIANFIGALGGGTGVLLTVSIVYRMYEQLLREKVSELHPAIAKLLNK	Q60175 UniProt Entry: SECY_METJA UniProt Gene: SECY, MJ0478 UniProt Name: Preprotein translocase secY subunit PIR Number:	1RHZ 1RH5 PDB Title: Preprotein translocase Secy subunit	van den Berg et al. (2004). van den Berg B, Clemons WM, Collinson I, Hartmann E, Harrison SC, & Rapoport TA (2004). X-ray structure of a protein-conducting channel. Nature 427 :36-44. PubMed Id: 14661030.
*SecY complex, beta subunit: Methanococcus jannaschii* A Archaea** SecG protein equivalent. Cytoplasm = in. Sequence from PDB. There is no sequence in Swiss-Prot. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.30,48; Sequence: MSKREETGLATSAGLIRYMDETFSKIRVKPEHVIGVTVAFVIIEAILTYGRFL		1RHZ 1RH5 PDB Title: Preprotein Translocase Secy Subunit	van den Berg et al. (2004). van den Berg B, Clemons WM, Collinson I, Hartmann E, Harrison SC, & Rapoport TA (2004). X-ray structure of a protein-conducting channel. Nature 427 :36-44. PubMed Id: 14661030.
*SecY complex, gamma subunit: Methanococcus jannaschii* A Archaea** SecE protein. Cytoplasm = in. Sequence from Swiss-Prot, with Met1 removed so that sequence corresponds to that in PDB. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.30,64; Sequence: KTDFNQKIEQLKEFIEECRRVWLVLKKPTKDEYLAVAKVTALGISLLGIIGYIIHVPATYIKGILKPPTTPRV	Q57817 UniProt Entry: SECE_METJA UniProt Gene: SECE, MJ0371 UniProt Name: Preprotein translocase secE subunit PIR Number:	1RHZ 1RH5 PDB Title: Preprotein Translocase Secy subunit	van den Berg et al. (2004). van den Berg B, Clemons WM, Collinson I, Hartmann E, Harrison SC, & Rapoport TA (2004). X-ray structure of a protein-conducting channel. Nature 427 :36-44. PubMed Id: 14661030.
Channels: Mechanosensitive
*MscL mechanosensor channel monomer: Mycobacterium tuberculosis* B Bacteria** Biological unit is a pentamer. Sequence from Swiss-Prot. TMhelices=2. N Terminal: in TM Segment Count: 2 TM Segments: A.15,39; B.71,89; Sequence: MLKGFKEFLARGNIVDLAVAVVIGTAFTALVTKFTDSIITPLINRIGVNAQSDVGILRIGIGGGQTIDLNVLLSAAINFFLIAFAVYFLVVLPYNTLRKKGEVEQPGDTQVVLLTEIRDLLAQTNGDSPGRHGGRGTPSPTDGPRASTESQ	P0A5K8 UniProt Entry: MSCL_MYCTU UniProt Gene: Large-conductance mechanosensitive channel UniProt Name: MSCL, RV0985C, MT1013, MTV044.13C PIR Number: E70821	2OAR PDB Title: mechanosensitive ion channel	Chang et al. (1998). Chang G, Spencer RH, Lee AT, Barclay MT, & Rees DC (1998). Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel. Science 282 :2220-2226. PubMed Id: 9856938.
*MscS mechanosensor channel monomer: Escherichia coli* B Bacteria** Biological unit is a heptamer. Sequence from Swiss-Prot. PDB sequence is truncated relative to Swiss-Prot. TMhelices=3. N Terminal: out TM Segment Count: 3 TM Segments: A.29,57; B.68,91; C.96,127; Sequence: MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRKIDATVADFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSREPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVWSNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRVKEDKAA	P0C0S1 UniProt Entry: MSCS_ECOLI UniProt Gene: mscS, B2924 UniProt Name: small-conductance mechanosensitive channel PIR Number: QQEC4	2OAU PDB Title: mechanosensitive channel protein	Bass et al. (2002). Bass RB, Strop P, Barclay M, & Rees DC (2002). Crystal Structure of Escherichia coli MscS, a Voltage-modulated and mechanosensitive channel. Science 298 :1582-1587. PubMed Id: 12446901.
Channels: Potassium, Sodium, & Proton Ion-Selective
*KcsA potassium channel : Streptomyces lividans B Bacteria** *The 'tmsegs' marked below include the so-called pore helix (P) associated with the pore region. 'tmseg' B corresponds to P. TMhelices=2. N Terminal: in TM Segment Count: 3 TM Segments: A.28,52; B.62,72; C.87,113; Sequence: MPPMLSGLLARLVKLLLGRHGSALHWRAAGAATVLLVIVLLAGSYLAVLAERGAPGAQLITYPRALWWSVETATTVGYGDLYPVTLWGRCVAVVVMVAGITSFGLVTAALATWFVGREQ	Q54397 UniProt Entry: KCSA_STRCO UniProt Gene: KCSA, SKC1, SCO7660, SC10F4.33 UniProt Name: Voltage-gated potassium channel PIR Number: S60172	1BL8 PDB Title: Potassium Channel (KcsA) from Streptomyces lividans	Doyle et al. (1998). Doyle DA, Cabral JM, Pfuetzner RA, Kuo AL, Gulbis JM, Cohen SL, Chait BT, & MacKinnon R (1998). The structure of the potassium channel: Molecular basis of K⁺conduction and selectivity. Science 280 :69-77. PubMed Id: 9525859.
*KvAP potassium channel : Aeropyrum pernix A Archaea** *The KvAP K-channel is complex. Of the 'tm segs' marked below, only tmsegs G and I are tmsegs in the usual sense. The others are associated with the pore helix and the voltage sensor domains. Using terminology from the Jiang et al. paper, the 'tmsegs' below have the following correspondence: A=S1, B=S2, C=S3a, D=S3b, E=S4, F=S4-S5 linker, G=S5, H=P, and I=S6. N Terminal: in TM Segment Count: 9 TM Segments: A.26,50; B.54,79; C.84,92; D.96,112; E.116,132; F.135,146; G.148,171; H.183,195; I.209,240; Sequence: MARFRRGLSDLGGRVRNIGDVMEHPLVELGVSYAALLSVIVVVVEYTMQLSGEYLVRLYLVDLILVIILWADYAYRAYKSGDPAGYVKKTLYEIPALVPAGLLALIEGHLAGLGLFRLVRLLRFLRILLIISRGSKFLSAIADAADKIRFYHLFGAVMLTVLYGAFAIYIVEYPDPNSSIKSVFDALWWAVVTATTVGYGDVVPATPIGKVIGIAVMLTGISALTLLIGTVSNMFQKILVGEPEPSCSPAKLAEMVSSMSEEEFEEFVRTLKNLRRLENSMK	Q9YDF8 UniProt Entry: below from TrEMBL UniProt Gene: APE0955 UniProt Name: 295AA long hypothetical potassium channel PIR Number:	1ORQ PDB Title: Voltage-Dependent Potassium Channel in complex with an Fab	Jiang et al. (2003). Jiang Y, Lee A, Chen J, Ruta V, Cadene M, Chait BT, & MacKinnon R (2003). X-ray structure of a voltage-dependent K⁺channel. Nature 423 :33-41. PubMed Id: 12721618. Crystal structures.
*MthK K+ channel : Methanobacterium thermoautotrophicum A Archaea** *The 'tmsegs' marked below include the so-called pore-helix (P) associated with the pore region. 'tmseg' B corresponds to P. Sequence from Swiss-Prot. TMhelices=2. N Terminal: in TM Segment Count: 3 TM Segments: A.19,40; B.49,57; C.72,95; Sequence: MVLVIEIIRKHLPRVLKVPATRILLLVLAVIIYGTAGFHFIEGESWTVSLYWTFVTIATVGYGDSPSTPLGMYFTVTLIVLGIGTFAVAVERLLEFLINREQMKLMGLIDVAKSRHVVICGWSESTLECLRELRGSEVFVLAEDENVRKKVLRSGANFVHGDPTRVSDLEKANVRGARAVIVDLESDSETIHCILGIRKIDESVRIIAEAERYENIEQLRMAGADQVISPFVISGRLMSRSIDDGYEAMFVQDVLAEESTRRMVEVPIPEGSKLEGVSVLDADIHDVTGVIIIGVGRGDELIIDPPRDYSFRAGDIILGIGKPEEIERLKNYISA	O27564 UniProt Entry: MTHK_METTH UniProt Gene: MTHK, MTH1520 UniProt Name: Calcium-gated potassium channel MthK PIR Number: H69069	1LNQ PDB Title: Potassium channel related protein	Jiang et al. (2002). Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R (2002). Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417 :515-22. PubMed Id: 12037559. Crystal structure and mechanism.
*KirBac1.1 potassium channel : Burkholderia pseudomallei B Bacteria** *The 'tmsegs' marked below include the so-called pore-helix (P) associated with the pore region, and the so-called slide-helix (Sl). For 'tmsegs' below, A corresponds to Sl and C to P. Sequence is from TrEMBL. TMhelices=2. N Terminal: in TM Segment Count: 4 TM Segments: A.47,51; B.60,81; C.98,104; D.121,149; Sequence: MNVDPFSPHSSDSFAQAASPARKPPRGGRRIWSGTREVIAYGMPASVWRDLYYWALKVSWPVFFASLAALFVVNNTLFALLYQLGDAPIANQSPPGFVGAFFFSVETLATVGYGDMHPQTVYAHAIATLEIFVGMSGIALSTGLVFARFARPRAKIMFARHAIVRPFNGRMTLMVRAANARQNVIAEARAKMRLMRREHSSEGYSLMKIHDLKLVRNEHPIFLLGWNMMHVIDESSPLFGETPESLAEGRAMLLVMIEGSDETTAQVMQARHAWEHDDIRWHHRYVDLMSDVDGMTHIDYTRFNDTEPVEPPGAAPDAQAFAAKPGEGDARPV	P83698 UniProt Entry: P83698 UniProt Gene: UniProt Name: potassium channel PIR Number:	1P7B PDB Title: potassium channel	Kuo et al (2003). Kuo A, Gulbis JM, Antcliff JF, Rahman T, Lowe ED, Zimmer J, Cuthbertson J, Ashcroft FM, Ezaki T, & Doyle DA (2003). Crystal structure of the potassium channel KirBac1.1 in the closed state. Science 300 :1922-1926. PubMed Id: 12738871.
*NaK channel, Na+ complex: Bacillus cereus* B Bacteria** Tetrameric form. Sequence for monomer from Swiss_Prot. N Terminal: in TM Segment Count: 2 TM Segments: A.22,44; B.74,102; Sequence: MLSFLLTLKRMLRACLRAWKDKEFQVLFVLTILTLISGTIFYSTVEGLRPIDALYFSVVTLTTVGDGNFSPQTDFGKIFTILYIFIGIGLVFGFIHKLAVNVQLPSILSNRKKE	Q81HW2 UniProt Entry: Q81HW2_BACCR UniProt Gene: BC_0669 UniProt Name: Potassium channel protein PIR Number:	2AHY PDB Title: Na+ complex of the NaK Channel	Shi et al. (2006). Shi N, Ye S, Alam A, Chen L, & Jiang Y (2006). Atomic structure of a Na+- and K+-conducting channel. Nature 440 :570-574. PubMed Id: 16467789.
Channels: Calcium Ion-Selective
Channels: Transient Receptor Potential (TRP) Non-selective cation channels responding to a wide range of chemical and physical stimuli
Channels: Gap Junctions and Related Channels
Channels: Other Ion Channels
Channels: Fluc Family These are F^--selective channels
Channels: Aquaporins and Glyceroporins
*aquaporin 1 : Homo sapiens E Eukaryota** One of the TM segments, C* + C, is composed of two end-to-end helical segments. The two partial segments are counted as 2 TM segments topologically. Sequence is from Swiss-Prot. TMhelices=6. N Terminal: in TM Segment Count: 8 TM Segments: A.8,36; B.49,66; C.77,84; D.95,115; E.137,155; F.167,183; *C.193,200; G.208,228; Sequence: MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLTGNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK	P29972 UniProt Entry: AQP1_HUMAN UniProt Gene: AQP1, CHIP28 UniProt Name: Aquaporin-CHIP PIR Number: A41616	1FQY PDB Title: aquaporin-1, chain A	Murata et al. (2000). Murata K, Mitsuoka K, Hirai T, Walz T, Agre P, Heymann J B, Engel A, & Fujiyoshi Y (2000). Structural determinants of water permeation through aquaporin-1. Nature 407 :599-605. PubMed Id: 11034202.
*aquaporin 1 : Bos taurus (Bovine) E Eukaryota** One of the TM segments, C* + C, is composed of two end-to-end helical segments. The two partial segments are counted as 2 TM segments topologically. Sequence is from Swiss-Prot. TMhelices=6. N Terminal: in TM Segment Count: 8 TM Segments: A.10,34; B.51,68; C.79,88; D.93,117; E.143,158; F.170,187; *C.194,204; G.216,230; Sequence: MASEFKKKLFWRAVVAEFLAMILFIFISIGSALGFHYPIKSNQTTGAVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISVLRAIMYIIAQCVGAIVATAILSGITSSLPDNSLGLNALAPGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSGPLAIGFSVALGHLLAIDYTGCGINPARSFGSSVITHNFQDHWIFWVGPFIGAALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK	P47865 UniProt Entry: AQP1_BOVIN UniProt Gene: AQP1 UniProt Name: Aquaporin-CHIP PIR Number: JC2348	1J4N PDB Title: aquaporin 1	Sui et al. (2001). Sui H, Han BG, Lee JK, Walian P, & Jap BK (2001). Structural basis of water-specific transport through the AQP1 water channel. Nature 414 :872-8. PubMed Id: 11780053.
*aquaporin Z : Escherichia coli B Bacteria** One of the TM segments, C* + C, is composed of two end-to-end helical segments. The two partial segments are counted as 2 TM segments topologically. Sequence is from Swiss-Prot. TMhelices=6. N Terminal: in TM Segment Count: 8 TM Segments: A.3,26; B.34,54; C.63,73; D.79,104; E.130,154; F.161,182; *C.186,198; G.206,225; Sequence: MFRKLAAECFGTFWLVFGGCGSAVLAAGFPELGIGFAGVALAFGLTVLTMAFAVGHISGGHFNPAVTIGLWAGGRFPAKEVVGYVIAQVVGGIVAAALLYLIASGKTGFDAAASGFASNGYGEHSPGGYSMLSALVVELVLSAGFLLVIHGATDKFAPAGFAPIAIGLALTLIHLISIPVTNTSVNPARSTAVAIFQGGWALEQLWFFWVVPIVGGIIGGLIYRTLLEKRD	P48838 UniProt Entry: AQPZ_ECOLI UniProt Gene: AQPZ, BNIP, B0875, C1009, SF0832, S0873 UniProt Name: Aquaporin Z PIR Number: C64826	1RC2 PDB Title: aquaporin Z	Savage et al. (2003). Savage DF, Egea PF, Robles-Colmenares Y, Iii JD, & Stroud RM (2003). Architecture and Selectivity in Aquaporins: 2.5 Å X-Ray Structure of Aquaporin Z. PLoS Biol 1 :334-340. PubMed Id: 14691544.
*Glycerol Channel, GlpF : Escherichia coli B Bacteria** One of the TM segments, C* + C, is composed of two end-to-end helical segments. The two partial segments are counted as 2 TM segments topologically. Sequence from Swiss-Prot. TMhelices=6. N Terminal: in TM Segment Count: 8 TM Segments: A.6,35; B.40,60; C.68,77; D.85,108; E.144,169; F.178,194; *C.204,217; G.232,254; Sequence: MSQTSTLKGQCIAEFLGTGLLIFFGVGCVAALKVAGASFGQWEISVIWGLGVAMAIYLTAGVSGAHLNPAVTIALWLFACFDKRKVIPFIVSQVAGAFCAAALVYGLYYNLFFDFEQTHHIVRGSVESVDLAGTFSTYPNPHINFVQAFAVEMVITAILMGLILALTDDGNGVPRGPLAPLLIGLLIAVIGASMGPLTGFAMNPARDFGPKVFAWLAGWGNVAFTGGRDIPYFLVPLFGPIVGAIVGAFAYRKLIGRHLPCDICVVEEKETTTPSEQKASL	P11244 UniProt Entry: GLPF_ECOLI UniProt Gene: GLPF, B3927, C4879, Z5472, ECS4852 UniProt Name: Glycerol uptake facilitator protein PIR Number: XMECGF	1FX8 PDB Title: Glycerol Uptake Facilitator Protein, Chain A	Fu et al. (2000). Fu D, Libson A, Miercke LJW, Weitzman C, Nollert P, Krucinski J, & Stroud RM (2000). Structure of a glycerol-conducting channel and the basis for its selectivity. Science 290 :481-486. PubMed Id: 11039922.
Channels : Formate/Nitrite Transporter (FNT) Family
Channels: Urea Transporters
Channels: Intercellular Channels found in sporulating bacteria that connect mother cell to forespore
Channels: Amt/Mep/Rh proteins
*ammonia transporter AmtB: Escherichia coli* B Bacteria** Sequence from PDB. Swiss-Prot sequence includes signal sequence (first 22 residues). Sequence below is from PDB and does not include signal sequence, therefore res#1 corresponds to res#23 in Swiss-Prot. N Terminal: out TM Segment Count: 11 TM Segments: A.7,33; B.38,68; C.96,120; D.125,148; E.163,182; F.195,221; G.224,253; H.256,275; I.280,306; J.310,334; K.347,380; Sequence: APAVADKADNAFMMICTALVLFMTIPGIALFYGGLIRGKNVLSMLTQVTVTFALVCILWVVYGYSLAFGEGNNFFGNINWLMLKNIELTAVMGSIYQYIHVAFQGSFACITVGLIVGALAERIRFSAVLIFVVVWLTLSYIPIAHMVWGGGLLASHGALDFAGGTVVHINAAIAGLVGAYLIGKRVGFGKEAFKPHNLPMVFTGTAILYIGWFGFNAGSAGTANEIAALAFVNTVVATAAAILGWIFGEWALRGKPSLLGACSGAIAGLVGVTPACGYIGVGGALIIGVVAGLAGLWGVTMLKRLLRVDDPCDVFGVHGVCGIVGCIMTGIFAASSLGGVGFAEGVTMGHQLLVQLESIAITIVWSGVVAFIGYKLADLTVGLRVPEEQEREGLDVNSHGENAYNA	P69681 UniProt Entry: AMTB_ECOLI UniProt Gene: amtB UniProt Name: ammonium channel PIR Number: A90692, C64775, E85542	1U7G PDB Title: Crystal structure of Ammonia Channel AmtB from E.Coli	Khademi et al. (2004). Khademi S, O'Connell J 3rd, Remis J, Robles-Colmenares Y, Miercke LJ, & Stroud RM (2004). Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 Å. Science 305 :1587-1594. PubMed Id: 15361618.
Cys-Loop Receptor Family Cation-selective and Anion-selective Ligand-gated Channels Cation-selective include nicotinic acetylcholine and serotonin 5-HT₃ receptors. Anion-selective include γ-aminobutyric, glycine, and invertebrate glutamate-gated chloride channels (GluCl)
*AChR pore alpha subunit: Torpedo marmorata* E Eukaryota** Sequence is from PDB, chain A. There is additional 24 AA as signal sequence in Swiss-Prot. TMhelices=4. N Terminal: in TM Segment Count: 4 TM Segments: A.211,237; B.243,271; C.275,300; D.403,436; Sequence: SEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLINVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVVNVIIPCLLFSFLTVLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIVTVVVINTHHRSPSTHTMPQWVRKIFINTIPNVMFFSTMKRASKEKQENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG	P02711 UniProt Entry: ACHA_TORMA UniProt Gene: CHRNA1 UniProt Name: Acetylcholine receptor subunit alpha PIR Number:	1OED PDB Title: Acetylcholine Receptor Protein, alpha Chain	Miyazawa et al. (2003). Miyazawa A, Fujiyoshi Y, & Unwin N (2003). Structure and gating mechanism of the acetylcholine receptor pore. Nature 423 :949-955. PubMed Id: 12827192.
*AChR pore beta subunit: Torpedo marmorata* E Eukaryota** Sequence is from PDB, chain B. There is additional 24 AA as signal sequence in Swiss-Prot. TMhelices=4. N Terminal: in TM Segment Count: 4 TM Segments: A.224,241; B.249,274; C.290,306; D.438,462; Sequence: SVMEDTLLSVLFENYNPKVRPSQTVGDKVTVRVGLTLTSLLILNEKNEEMTTSVFLNLAWTDYRLQWDPAAYEGIKDLSIPSDDVWQPDIVLMNNNDGSFEITLHVNVLVQHTGAVSWHPSAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEVILQHALDAKGEREVKEIMINQDAFTENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRKPLFYIVYTIVPCILISILAILVFYLPPDAGEKMSLSISALLALTVFLLLLADKVPETSLSVPIIISYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPVTTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVTLPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYIFITMCSIGTFSIFLDASHNVPPDNPFA	Q6S3I0 UniProt Entry: Q6S3I0_TORMA UniProt Gene: none UniProt Name: Acetylcholine receptor beta subunit PIR Number:	1OED PDB Title: Acetylcholine Receptor Protein, beta Chain	Miyazawa et al. (2003). Miyazawa A, Fujiyoshi Y, & Unwin N (2003). Structure and gating mechanism of the acetylcholine receptor pore. Nature 423 :949-955. PubMed Id: 12827192.
*AChR pore gamma subunit: Torpedo marmorata* E Eukaryota** Sequence is from PDB, chain E. Sequence in PDB has first 16 AA removed relative to Swiss-Prot. TMhelices=4. N Terminal: in TM Segment Count: 4 TM Segments: A.221,246; B.250,280; C.286,311; D.446,478; Sequence: NEEGRLIEKLLGDYDKRIKPAKTLDHVIDVTLKLTLTNLISLNEKEEALTTNVWIEIQWNDYRLSWNTSEYEGIDLVRIPSELLWLPDVVLENNVDGQFEVAYYANVLVYNDGSMYWLPPAIYRSTCPIAVTYFPFDWQNCSLVFRSQTYNAHEVNLQLSAEEGEVVEWIHIDPEDFTENGEWTIRHRPAKKNYNWQLTKDDIDFQEIIFFLIIQRKPLFYIINIIAPCVLISSLVVLVYFLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSLVIVTNCVIVLNVSLRTPNTHSLSEKIKHLFLEFLPKYLGMHLEPSEETPEKPQPRRRSSFGIMIKAEEYILKKPRSELMFEEQKDRHGLKRVNKMTSDIDIGTTVDLYKDLANFAPEIKSCVEACNFIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSLGTLAIFLTGHLNQVPEFPFPGDPRKYVP	Q6S3H9 UniProt Entry: Q6S3H9_TORMA UniProt Gene: none UniProt Name: Acetylcholine receptor gamma subunit PIR Number:	1OED PDB Title: Acetylcholine Receptor Protein, gamma Chain	Miyazawa et al. (2003). Miyazawa A, Fujiyoshi Y, & Unwin N (2003). Structure and gating mechanism of the acetylcholine receptor pore. Nature 423 :949-955. PubMed Id: 12827192.
*AChR pore delta subunit: Torpedo marmorata* E Eukaryota** Sequence is from PDB, chain C. Sequence in PDB has first 21 AA removed relative to Swiss-Prot. TMhelices=4. N Terminal: in TM Segment Count: 4 TM Segments: A.226,253; B.257,285; C.289,316; D.452,483; Sequence: VNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTTNVWMDHAWYDHRLTWNASEYSDISILRLRPELIWIPDIVLQNNNDGQYNVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYNANEISMDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYGDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLAALAFYLPAESGEKMSTAICVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVVVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRVDEIEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNRPPAKPFEGDPFDYSSDHPRCA	Q6S3H8 UniProt Entry: Q6S3H8_TORMA UniProt Gene: none UniProt Name: Acetylcholine receptor delta subunit PIR Number:	1OED PDB Title: Acetylcholine Receptor Protein, delta Chain	Miyazawa et al. (2003). Miyazawa A, Fujiyoshi Y, & Unwin N (2003). Structure and gating mechanism of the acetylcholine receptor pore. Nature 423 :949-955. PubMed Id: 12827192.
Type VII Secretion Systems
G PROTEIN-COUPLED RECEPTORS (GPCRs) Wikipedia Entry GPCRdb Home Page GPCR Molecular Dynamics Database
G Protein-Coupled Receptors: Class A
*rhodopsin: Bos taurus (Bovine)* E Eukaryota** Sequence from Swiss-Prot. TMhelices=7. N Terminal: out TM Segment Count: 7 TM Segments: A.35,64; B.71,100; C.107,139; D.151,173; E.200,225; F.247,277; G.286,306; Sequence: MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA	P02699 UniProt Entry: OPSD_BOVIN UniProt Gene: RHO UniProt Name: Rhodopsin PIR Number: OOBO	1F88 PDB Title: crystal structure of bovine rhodopsin - Chain A, B	Palczewski et al. (2000). Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, & Miyano M (2000). Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289 :739-745. PubMed Id: 10926528.
G Protein-Coupled Receptors: Class B1
G Protein-Coupled Receptors: Class B2
G Protein-Coupled Receptors: Class C
G Protein-Coupled Receptors: Class D These are found exclusively in fungi
G Protein-Coupled Receptors: Class F
G Protein-Coupled Receptors: Class T
Wntless (WLS) Transporters Also called Evi and GPR177 transporters.
Host-Defense Proteins
H⁺/Cl^- or F^- Exchange Transporters
*ClC chloride channel : Salmonella typhimurium B Bacteria** *The topology of this protein is complex! The 'tmsegs' are all helical segments buried witin the protein and membrane. Check original papers for details. Sequence is from Swiss-Prot. TMhelices=14 (based on turn reversals). N Terminal: in TM Segment Count: 17 TM Segments: A.33,70; B.77,99; C.108,116; D.123,141; E.148,166; F.171,189; G.193,203; H.213,233; I.254,283; J.288,306; K.320,323; L.329,350; M.356,377; N.386,402; O.404,416; P.421,439; Q.442,458; Sequence: MKTDTSTFLAQQIVRLRRRDQIRRLMQRDKTPLAILFMAAVVGTLTGLVGVAFEKAVSWVQNMRIGALVQVADHAFLLWPLAFILSALLAMVGYFLVRKFAPEAGGSGIPEIEGALEELRPVRWWRVLPVKFIGGMGTLGAGMVLGREGPTVQIGGNLGRMVLDVFRMRSAEARHTLLATGAAAGLSAAFNAPLAGILFIIEEMRPQFRYNLISIKAVFTGVIMSSIVFRIFNGEAPIIEVGKLSDAPVNTLWLYLILGIIFGCVGPVFNSLVLRTQDMFQRFHGGEIKKWVLMGGAIGGLCGILGLIEPAAAGGGFNLIPIAAAGNFSVGLLLFIFITRVVTTLLCFSSGAPGGIFAPMLALGTLLGTAFGMAAAVLFPQYHLEAGTFAIAGMGALMAASVRAPLTGIVLVLEMTDNYQLILPMIITCLGATLLAQFLGGKPLYSTILARTLAKQDAEQAEKNQNAPADENT	Q8ZRP8 UniProt Entry: CLCA_SALTY UniProt Gene: CLCA, ERIC, STM0203 UniProt Name: Voltage-gated ClC-type chloride channel clcA PIR Number:	1KPL PDB Title: ClC chloride channel	Dutzler et al. (2002). Dutzler R, Campbell EB, Cadene M, Chait BT, & MacKinnon R (2002). X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 415 :287-294. PubMed Id: 11796999.
*ClC chloride channel : Escherichia coli B Bacteria** *The topology of this protein is complex! The 'tmsegs' are all helical segments buried within the protein and membrane. Check original papers for details. Sequence is from Swiss-Prot. TMhelices=14 (based on turn reversals). N Terminal: in TM Segment Count: 17 TM Segments: A.33,70; B.77,99; C.108,116; D.123,141; E.148,166; F.171,189; G.193,203; H.213,233; I.254,283; J.288,306; K.320,323; L.329,350; M.356,377; N.386,402; O.404,416; P.421,439; Q.442,458; Sequence: MKTDTPSLETPQAARLRRRQLIRQLLERDKTPLAILFMAAVVGTLVGLAAVAFDKGVAWLQNQRMGALVHTADNYPLLLTVAFLCSAVLAMFGYFLVRKYAPEAGGSGIPEIEGALEDQRPVRWWRVLPVKFFGGLGTLGGGMVLGREGPTVQIGGNIGRMVLDIFRLKGDEARHTLLATGAAAGLAAAFNAPLAGILFIIEEMRPQFRYTLISIKAVFIGVIMSTIMYRIFNHEVALIDVGKLSDAPLNTLWLYLILGIIFGIFGPIFNKWVLGMQDLLHRVHGGNITKWVLMGGAIGGLCGLLGFVAPATSGGGFNLIPIATAGNFSMGMLVFIFVARVITTLLCFSSGAPGGIFAPMLALGTVLGTAFGMVAVELFPQYHLEAGTFAIAGMGALLAASIRAPLTGIILVLEMTDNYQLILPMIITGLGATLLAQFTGGKPLYSAILARTLAKQEAEQLARSKAASASENT	P37019 UniProt Entry: CLCA_ECOLI UniProt Gene: CLCA, ERIC, B0155 UniProt Name: Voltage-gated ClC-type chloride channel clcA PIR Number: C64739	1KPK 1OTS PDB Title: ClC chloride channel	Dutzler et al. (2002). Dutzler R, Campbell EB, Cadene M, Chait BT, & MacKinnon R (2002). X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 415 :287-294. PubMed Id: 11796999.
AAA-ATPAse Membrane Translocators AAA: ATPases associated with various cellular activities
Stomatin, Prohibitin, Flotillin, and HflK/C (SPFH) Family Proteins These proteins seem to play a scaffolding role microdomain formation.
Celluose Synthases Membrane Imbedded Glycosyltransferases These use UDP-activated glucose to elongate nascent polysaccharides processively across membranes.
PNPT Superfamily PNPT: polyprenylphosphate N-acetyl hexosamine 1-phosphate transferase Proteins in this superfamily are responsible for the synthesis of cell envelope polymers
Shape, Elongation, Division, and Sporulation (SEDS) Proteins
Oligosaccharyltransferases (OST) Catalyses Asparagine-linked (N-linked) Glycosylation
Protein O-mannosyltransferases (POMT/PMT) POMT in mammals or PMT in yeast
Glycosyltransfereases
Glucosyltransferases
Chain Length Determinant and Associated Proteins Chain-length determinant protein involved in lipopolysaccharide synthesis
Phospholipid Synthases
Diacylglyceryl Transferases
Liponucleotide Synthetases Cytidine-Diphosphate Diacylglycerol Synthetase is the prominent member of the family
N-acyltransferases
O-acyltransferases Membrane-bound O-acyltransferases (MBOATS)
O-Phosphatidyl Transferases
S-acyltransferases Eukaryotic proteins that catalyze protein palmitoylation
Phospholipid Transferases Includes phosphoethanolamine (PEA) transferases and cardiolipin transferases involved in the assembly of outer membranes
Very Long Chain Fatty Acid Elongases
Methyltransferases
Phosphotransferases
Phosphatidic Acid Phosphatases Membrane-integrated type II phosphatidic acid phosphatases (PAP2)
UbiA Prenyltransferases These enzymes are involved in the biosynthesis of a wide range molecules, including respiratory lipoquinones and archael lipids
Phosphoenolpyruvate-Dependent Phosphotransferases (PTSs)
Intramembrane Proteases ( NSMB News & Views on three GlpG Structures)
*Rhomboid Protease GlpG: Escherichia coli* B Bacteria** Sequence from Swiss-Prot. N Terminal: out TM Segment Count: 6 TM Segments: A.95,114; B.148,169; C.171,193; D.201,217; E.227,241; F.251,268; Sequence: MLMITSFANPRVAQAFVDYMATQGVILTIQQHNQSDVWLADESQAERVRAELARFLENPADPRYLAASWQAGHTGSGLHYRRYPFFAALRERAGPVTWVMMIACVVVFIAMQILGDQEVMLWLAWPFDPTLKFEFWRYFTHALMHFSLMHILFNLLWWWYLGGAVEKRLGSGKLIVITLISALLSGYVQQKFSGPWFGGLSGVVYALMGYVWLRGERDPQSGIYLQRGLIIFALIWIVAGWFDLFGMSMANGAHIAGLAVGLAMAFVDSLNARKRK	GLPG_ECOLI UniProt Entry: P09391 UniProt Gene: glpG UniProt Name: Protein glpG PIR Number:	2IC8 PDB Title: Crystal structure of GlpG	Wang et al. (2006). Wang Y, Zhang Y, & Ha Y (2006). Crystal structure of a rhomboid family intramembrane protease. Nature 444 :179-183. PubMed Id: 17051161.
*Rhomboid peptidase: Haemophilus influenzae* B Bacteria** Sequence from Swiss-Prot. TM E is unusual in that it is not fully alpha helical but rather is deformed. check orginal article for details. N Terminal: in TM Segment Count: 6 TM Segments: A.10,26; B.63,84; C.86,108; D.116,131; E.137,156; F.166,191; Sequence: MKNFLAQQGKITLILTALCVLIYLAQQLGFEDDIMYLMHYPAYEEQDSEVWRYISHTLVHLSNLHILFNLSWFFIFGGMIERTFGSVKLLMLYVVASAITGYVQNYVSGPAFFGLSGVVYAVLGYVFIRDKLNHHLFDLPEGFFTMLLVGIALGFISPLFGVEMGNAAHISGLIVGLIWGFIDSKLRKNSLE	P44783 UniProt Entry: GLPG_HAEIN UniProt Gene: glpG UniProt Name: Protein glpG homolog PIR Number: I64081	2NR9 PDB Title: Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae	Lemieux et al. (2007). Lemieux MJ, Fischer SJ, Cherney MM, Bateman KS, & James MNG (2007). The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis. Proc Natl Acad Sci USA 104 :750-754. PubMed Id: 17210913.
Cysteine Proteases Also known as Thiol Proteases
Membrane-Bound Metalloproteases
CorA Superfamily Ion Transporters Channels and transporters for divalent cation homeostasis. These have a membrane domain in series with a cytoplasmic domain that together form a continuous channel.
*CorA Mg2+ transporter: Thermotoga maritima* B Bacteria** Pentameric form. Sequence for monomer from PDB. See also later structure 2IUB. N Terminal: in TM Segment Count: 2 TM Segments: A.291,312; B.326,345; Sequence: MEEKRLSAKKGLPPGTLVYTGKYREDFEIEVMNYSIEEFREFKTTDVESVLPFRDSSTPTWINITGIHRTDVVQRVGEFFGIHPLVLEDILNVHQRPKVEFFENYVFIVLKMFTYDKNLHELESEQVSLILTKNCVLMFQEKIGDVFDPVRERIRYNRGIIRKKRADYLLYSLIDALVDDYFVLLEKIDDEIDVLEEEVLERPEKETVQRTHQLKRNLVELRKTIWPLREVLSSLYRDVPPLIEKETVPYFRDVYDHTIQIADTVETFRDIVSGLLDVYLSSVSNKTNEVMKVLTIIATIFMPLTFIAGIYGMNFEYMPELRWKWGYPVVLAVMGVIAVIMVVYFKKKKWL	Q9WZ31 UniProt Entry: CORA_THEMA UniProt Gene: corA UniProt Name: Magnesium transport protein corA PIR Number: H72360	2BBH PDB Title: X-ray structure of T. maritima CorA soluble domain	Lunin et al. (2006). Lunin VV, Dobrovetsky E, Khutoreskaya G, Zhang R, Joachimiak A, Doyle DA, Bochkarev A, Maguire ME, Edwards AM, & Koth CM (2006). Crystal structure of the CorA Mg²⁺transporter. Nature 440 :833-837. PubMed Id: 16598263.
Cyclin M/CorC Family of Mg²⁺ Transporters Cyclin M is generally abbreviated CNNM. Reviewed by Funato & Miki (2019)
Bacterial Mercury Detoxification Proteins
Rhodaneses Thiosulfate-Cyanide sulfurtransfereases
Drug/Metabolite Transporter (DMT) Superfamily
Multiple Peptide Resistance Factors (MprFs) These proteins use two separate domains to synthesize and translocate aminoacyl phospholipids
Multi-Drug Efflux Transporters Members of the multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) transporter superfamily
*AcrB multidrug transporter: Escherichia coli* B Bacteria** Sequence from Swiss-Prot. TMhelices=12. N Terminal: in TM Segment Count: 12 TM Segments: A.11,29; B.331,356; C.367,386; D.395,421; E.439,457; F.465,497; G.537,557; H.873,892; I.896,919; J.925,954; K.972,990; L.999,1021; Sequence: MPNFFIDRPIFAWVIAIIIMLAGGLAILKLPVAQYPTIAPPAVTISASYPGADAKTVQDTVTQVIEQNMNGIDNLMYMSSNSDSTGTVQITLTFESGTDADIAQVQVQNKLQLAMPLLPQEVQQQGVSVEKSSSSFLMVVGVINTDGTMTQEDISDYVAANMKDAISRTSGVGDVQLFGSQYAMRIWMNPNELNKFQLTPVDVITAIKAQNAQVAAGQLGGTPPVKGQQLNASIIAQTRLTSTEEFGKILLKVNQDGSRVLLRDVAKIELGGENYDIIAEFNGQPASGLGIKLATGANALDTAAAIRAELAKMEPFFPSGLKIVYPYDTTPFVKISIHEVVKTLVEAIILVFLVMYLFLQNFRATLIPTIAVPVVLLGTFAVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVMAEEGLPPKEATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGSTGAIYRQFSITIVSAMALSVLVALILTPALCATMLKPIAKGDHGEGKKGFFGWFNRMFEKSTHHYTDSVGGILRSTGRYLVLYLIIVVGMAYLFVRLPSSFLPDEDQGVFMTMVQLPAGATQERTQKVLNEVTHYYLTKEKNNVESVFAVNGFGFAGRGQNTGIAFVSLKDWADRPGEENKVEAITMRATRAFSQIKDAMVFAFNLPAIVELGTATGFDFELIDQAGLGHEKLTQARNQLLAEAAKHPDMLTSVRPNGLEDTPQFKIDIDQEKAQALGVSINDINTTLGAAWGGSYVNDFIDRGRVKKVYVMSEAKYRMLPDDIGDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKSTGEAMELMEQLASKLPTGVGYDWTGMSYQERLSGNQAPSLYAISLIVVFLCLAALYESWSIPFSVMLVVPLGVIGALLAATFRGLTNDVYFQVGLLTTIGLSAKNAILIVEFAKDLMDKEGKGLIEATLDAVRMRLRPILMTSLAFILGVMPLVISTGAGSGAQNAVGTGVMGGMVTATVLAIFFVPVFFVVVRRRFSRKNEDIEHSHTVDHH	P31224 UniProt Entry: ACRB_ECOLI UniProt Gene: ACRB, ACRE, B0462 UniProt Name: Acriflavine resistance protein B PIR Number: B36938	1IWG PDB Title: multidrug efflux transporter Acrb	Murakami et al. (2002). Murakami S, Nakashima R, Yamashita E, & Yamaguchi A (2002). Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419 :587-593. PubMed Id: 12374972.
AbgT Family of Transporters Involved in bacterial folate synthesis through catabolite transport Proteins in this family may also function as drug efflux pumps
Sulfate-Uptake Transporters/Permeases
Membrane-Associated Proteins in Eicosanoid and Glutathione Metabolism (MAPEG)
SWEET and semiSWEET Transporters, and Their Relatives SWEETs are monsaccharide and disaccharide transporters. Bacterial homologues are semiSWEETS.
Aluminum-Activated Malate Transporter Family (ALMTs)
Neurotransmitter Sodium Symporter (NSS) Family NSS family catalyze uptake of a variety of neurotransmitters, amino acids, and osmolytes
Amino Acid Secondary Transporters
Solute Carrier (SLC) Transporter Superfamily Active transporters that use Na⁺ or H⁺ electrochemical gradients Fold Atlas of the Human SLC Superfamily Xie et al. (2022)
Translocator Protein (18 kDA) TSPO Principally an outer mitochondrial membrane protein that binds to cholesterol and drug ligands, but occurs in diverse organisms Previously referred to as a peripheral-type benzodiazepine receptor (PBR). In mitochondria, it is part of large multimeric complex located in the outer mitochondrial membrane, and is closely associated with VDAC.
Ca²⁺:Cation Antiporter (CaCA) Family
Nucleobase-Cation-Symport-1 (NCS1) Family
Nucleobase-Cation-Symport-2 (NCS2) Family also known as nucleobase/ascorbate transporter (NAT)
Solute Carrier Family 4 (anion exchanger)
Betaine/Choline/Carnitine Transporter (BCCT) Family
Amino Acid/Polyamine/Organocation (APC) Superfamily
Cation Diffusion Facilitator (CDF) Family
Antiporters
*Na+_H+_antiporter: Escherichia coli* B Bacteria** Sequence from PDB. TM segment D and K consists two short alpha-Helices N Terminal: in TM Segment Count: 12 TM Segments: A.12,30; B.59,85; C.95,116; D.121,143; E.150,175; F.182,200; G.205,218; H.223,236; I.247,271; J.290,311; K.327,350; L.357,382; Sequence: MKHLHRFFSSDASGGIILIIAAILAMIMANSGATSGWYHDFLETPVQLRVGSLEINKNMLLWINDALMAVFFLLVGLEVKRELMQGSLASLRQAAFPVIAAIGGMIVPALLYLAFNYADPITREGWAIPAATDIAFALGVLALLGSRVPLALKIFLMALAIIDDLGAIIIIALFYTNDLSMASLGVAAVAIAVLAVLNLCGARRTGVYILVGVVLWTAVLKSGVHATLAGVIVGFFIPLKEKHGRSPAKRLEHVLHPWVAYLILPLFAFANAGVSLQGVTLDGLTSILPLGIIAGLLIGKPLGISLFCWLALRLKLAHLPEGTTYQQIMVVGILCGIGFTMSIFIASLAFGSVDPELINWAKLGILVGSISSAVIGYSWLRVRLRPSV	P13738 UniProt Entry: NHAA_ECOLI UniProt Gene: nhaA UniProt Name: Na(+)/H(+) antiporter 1 PIR Number: C64722	1ZCD PDB Title: Crystal structure of the Na+/H+ antiporter NhaA	Hunte et al. (2005). Hunte C, Screpanti E, Venturi M, Rimon A, Padan E, & Michel H (2005). Structure of a Na(+)/H(+) antiporter and insights into mechanism of action and regulation by pH. Nature 435 :1197-1202. PubMed Id: 15988517.
*ADP/ATP carrier protein : Bos taurus (Bovine) E Eukaryota** *The helices form a deep, broad cavity lined with polar residues. This means that some of the TM segments are quite polar. Sequence from Swiss-Prot. TMhelices=6. N Terminal: out TM Segment Count: 6 TM Segments: A.4,37; B.73,99; C.108,142; D.176,199; E.209,238; F.273,290; Sequence: SDQALSFLKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFTGLGNCITKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQTVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGPKAFFKGAWSNVLRGMGGAFVLVLYDEIKKFV	P02722 UniProt Entry: ADT1_BOVIN UniProt Gene: SLC25A4, ANT1 UniProt Name: ADP,ATP carrier protein, heart isoform T1 PIR Number: A43646, XWBO	1OKC PDB Title: ADP, ATP carrier protein heart isoform T1	Pebay-Peyroula et al. (2003). Pebay-Peyroula E, Dahout-Gonzalez C, Kahn R, Trezeguet V, Lauquin GJ, & Brandolin G (2003). Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside. Nature 426 :39-44. PubMed Id: 14603310.
Apical Sodium-Dependent Bile Acid Transporters (ASBT) Closely related to sodium taurocholate co-transporting polypeptide (NTCP). Both proteins are members of SLC10 solute carrier family
Energy-Coupling Factor (ECF) Transporters
ATP Binding Cassette (ABC) Transporters Reviewed by Hou et al. (2022)
*BtuCD ABC transporter, BtuC subunit: Escherichia coli* B Bacteria** TM helix G does not cross the membrane completely. It ends in an extended stretch packed between several other helices. Functional protein has 2 BtuC subunits (membrane spanning) & 2 BtuD subunits. Not all TM segments are fully helical. Sequence from Swiss-Prot. TMhelices=10. N Terminal: in TM Segment Count: 10 TM Segments: A.2,32; B.47,81; C.93,107; D.114,138; E.142,166; F.191,206; G.229,249; H.258,267; I.272,296; J.305,324; Sequence: MLTLARQQQRQNIRWLLCLSVLMLLALLLSLCAGEQWISPGDWFSPRGELFVWQIRLPRTLAVLLVGAALAISGAVMQALFENPLAEPGLLGVSNGAGVGLIAAVLLGQGQLPNWALGLCAIAGALIITLILLRFARRHLSTSRLLLAGVALGIICSALMTWAIYFSTSVDLRQLMYWMMGGFGGVDWRQSWLMLALIPMLLWICCQSRPMNMLALGEISARQLGLPLWFWRNVLVAATGWMVGVSVALAGAIGFIGLVIPHILRLCGLTDHRALLPGCALAGASALLLADIVARLALAAAELPIGVVTATLGAPVFIWLLLKAGR	Q8X4L7 UniProt Entry: BTUC_ECO57 UniProt Gene: BTUC, Z2740, ECS2418 UniProt Name: Vitamin B12 transport system permease protein btuC PIR Number: B90931	1L7V PDB Title: bacterial ABC transporter involved in B12 uptake	Locher et al. (2002). Locher KP, Lee AT, & Rees DC (2002). The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism. Science 296 :1091-1098. PubMed Id: 12004122.
Tripartite ATP-independent periplasmic (TRAP) protein family
Major Facilitator Superfamily (MFS) Transporters
*lactose permease, 3D structure: Escherichia coli* B Bacteria** protein is a mutant:C154G. Sequence is thus from PDB file. TMhelices=12. N Terminal: in TM Segment Count: 12 TM Segments: A.6,34; B.42,70; C.75,100; D.104,136; E.140,164; F.166,186; G.221,247; H.254,276; I.288,304; J.312,340; K.343,376; L.378,399; Sequence: MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQPLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNAGAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALGASIVGIMFTINNQFVFWLGSGCALILAVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFDQQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMSVRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQLAMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVA	P02920 UniProt Entry: LACY_ECOLI UniProt Gene: LACY, B0343 UniProt Name: Lactose permease PIR Number: GREC	1PV6 1PV7 PDB Title: Lactose Permease	Abramson et al. (2003). Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, & Iwata S (2003). Structure and mechanism of the lactose permease of Escherichia coli. Science 301 :610-615. PubMed Id: 12893935.
*glycerol-3-phosphate transporter: Escherichia coli* B Bacteria** sequence is from Swiss-Prot, which differs somewhat from PDB. Sequence numbering in PDB corresponds to Swiss-Prot sequence. TMhelices=12. N Terminal: in TM Segment Count: 12 TM Segments: A.20,57; B.64,88; C.94,112; D.121,147; E.153,180; F.190,207; G.253,282; H.288,316; I.322,341; J.347,374; K.380,409; L.415,448; Sequence: MLSIFKPAPHKARLPAAEIDPTYRRLRWQIFLGIFFGYAAYYLVRKNFALAMPYLVEQGFSRGDLGFALSGISIAYGFSKFIMGSVSDRSNPRVFLPAGLILAAAVMLFMGFVPWATSSIAVMFVLLFLCGWFQGMGWPPCGRTMVHWWSQKERGGIVSVWNCAHNVGGGIPPLLFLLGMAWFNDWHAALYMPAFCAILVALFAFAMMRDTPQSCGLPPIEEYKNDYPDDYNEKAEQELTAKQIFMQYVLPNKLLWYIAIANVFVYLLRYGILDWSPTYLKEVKHFALDKSSWAYFLYEYAGIPGTLLCGWMSDKVFRGNRGATGVFFMTLVTIATIVYWMNPAGNPTVDMICMIVIGFLIYGPVMLIGLHALELAPKKAAGTAAGFTGLFGYLGGSVAASAIVGYTVDFFGWDGGFMVMIGGSILAVILLIVVMIGEKRRHEQLLQERNGG	P08194 UniProt Entry: GLPT_ECOLI UniProt Gene: Glycerol-3-phosphate transporter UniProt Name: GLPT or B2240 PIR Number: JNECGT	1PW4 PDB Title: Glycerol-3-phosphate transporter	Abramson et al. (2003). Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, & Iwata S (2003). Structure and mechanism of the lactose permease of Escherichia coli. Science 301 :610-615. PubMed Id: 12893935.
*multidrug resistance protein EmrD: Escherichia coli* B Bacteria** Sequence from Swiss-Prot N Terminal: in TM Segment Count: 12 TM Segments: A.9,35; B.43,68; C.72,91; D.99,125; E.133,155; F.161,178; G.203,230; H.236,261; I.267,285; J.290,312; K.320,349; L.356,378; Sequence: MKRQRNVNLLLMLVLLVAVGQMAQTIYIPAIADMARDLNVREGAVQSVMGAYLLTYGVSQLFYGPISDRVGRRPVILVGMSIFMLATLVAVTTSSLTVLIAASAMQGMGTGVGGVMARTLPRDLYERTQLRHANSLLNMGILVSPLLAPLIGGLLDTMWNWRACYLFLLVLCAGVTFSMARWMPETRPVDAPRTRLLTSYKTLFGNSGFNCYLLMLIGGLAGIAAFEACSGVLMGAVLGLSSMTVSILFILPIPAAFFGAWFAGRPNKRFSTLMWQSVICCLLAGLLMWIPDWFGVMNVWTLLVPAALFFFGAGMLFPLATSGAMEPFPFLAGTAGALVGGLQNIGSGVLASLSAMLPQTGQGSLGLLMTLMGLLIVLCWLPLATRMSHQGQPV	P31442 UniProt Entry: EMRD_ECOLI UniProt Gene: emrD UniProt Name: Multidrug resistance protein D PIR Number:	2GFP PDB Title: Structure of the Multidrug Transporter EmrD from Escherichia coli	Yin et al. (2006). Yin Y, He X, Szewczyk P, Nguyen T, & Chang G. (2006). Structure of the multidrug transporter EmrD from Escherichia coli. Science 312 :741-744. PubMed Id: 16675700.
Solute Sodium Symporter (SSS) Family
PIN-FORMED (PIN) Auxin Efflux Carriers and Related Proteins PIN-FORMED refers to the phenotype of the pin1 mutant. Plants with this mutation fail to flower properly.
CDP-Alcohol Phosphotransferases These enzymes facilitate the conjugation of polar headgroups to diacylglycerol lipid tails
Insulin-Induced Gene Products: Insig Proteins These are components of the sterol regulatory element-binding protein (SREBP) pathway
Sterol Reductases
HMG CoA Reductase 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR)
Sterol Isomerases
Sterol-Sensing Domain (SSD) Proteins These proteins are involved in cholesterol trafficking in the cholesterol-uptake pathway
Fatty Acid Desaturases These enzymes maintain the cellular balance of saturated and monounsaturated lipids
Superfamily of K⁺ Transporters (SKT proteins)
Membrane-Integral Pyrophosphatases (M-PPases) Ion-Translocating Pyrophosphatases Link Pyrophosphate (PP_i) Hydrolysis to Sodium or Proton Pumping V-ATPases and H⁺-PPases coexist on plant vacuolar membranes
Vacuolar Iron Transporter (VIT) Family These proteins transport cytoplasmic ferrous ions into vacuoles
Bacterial V-type ATPase Also called A-type ATPase
Vacuolar ATPase (V-ATPase) Eukaryotic V-ATPases
Flagellar Motor Proteins
F-type ATPase
*F1F0 ATPsynthase Subunit C: Escherichia coli* B Bacteria** Sequence is from Swiss-Prot. For context of this protein, see 1QO1 (ATP synthase rotary motor). TMhelices=2. N Terminal: out TM Segment Count: 2 TM Segments: A.2,39; B.47,77; Sequence: MENLNMDLLYMAAAVMMGLAAIGAAIGIGILGGKFLEGAARQPDLIPLLRTQFFIVMGLVDAIPMIAVGLGLYVMFAVA	P00844 UniProt Entry: ATPL_ECOLI UniProt Gene: ATPE, UNCE, PAPH, B3737, C4665, Z5235, ECS4679, STM3870, STY3908, SF3817, YPO4126, Y4140 UniProt Name: ATP synthase C chain PIR Number: LWECA	1A91 PDB Title: F1F0 Atpase Subunit C	Girvin et al. (1998). Girvin ME, Rastogi VK, Abildgaard F, Markley JL, & Fillingame RH (1998). Solution structure of the transmembrane H⁺-transporting subunit c of the F₁F₀ ATP synthase. Biochemistry 37 :8817-8824. PubMed Id: 9636021. doi:10.1021/bi980511m.
*F-type Na+-ATPase Subunit C: Ilyobacter tartaricus* B Bacteria** Homodimer. Sequence for monomer from Swiss-Prot. For context of this protein, see 1QO1 (ATP synthase rotary motor) N Terminal: out TM Segment Count: 2 TM Segments: A.4,44; B.48,80; Sequence: MDMLFAKTVVLAASAVGAGTAMIAGIGPGVGQGYAAGKAVESVARQPEAKGDIISTMVLGAVAESTGIYSLVIALILLYANPFVGLLG	Q8KRV3 UniProt Entry: Q8KRV3_9FUSO UniProt Gene: atpE UniProt Name: Subunit C PIR Number:	1YCE PDB Title: Structure of the rotor ring of F-type Na+-ATPase from Ilyobacter tartaricus	Meier et al. (2005). Meier T, Polzer P, Diederichs K, Welte W, & Dimroth P (2005). Structure of the rotor ring of F-type Na-ATPase from Ilyobacter tartaricus. Science 308 :659-662. PubMed Id: 15860619.
P-type ATPase
*Ca ATPase, SR: Oryctolagus cuniculus (Rabbit)* E Eukaryota** helix E protrudes into a soluble domain. Nterm in = cytoplasm, out = SR lumen. Sequence is from Swiss-Prot. PDB sequence is C-terminus truncated/modified. TMhelices=10. N Terminal: in TM Segment Count: 10 TM Segments: A.48,80; B.89,119; C.247,274; D.289,307; E.739,779; F.788,809; G.830,852; H.893,912; I.930,950; J.964,986; Sequence: MEAAHSKSTEECLAYFGVSETTGLTPDQVKRHLEKYGHNELPAEEGKSLWELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIANAIVGVWQERNAENAIEALKEYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILSIKSTTLRVDQSILTGESVSVIKHTEPVPDPRAVNQDKKNMLFSGTNIAAGKALGIVATTGVSTEIGKIRDQMAATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCKMFIIDKVDGDFCSLNEFSITGSTYAPEGEVLKNDKPIRSGQFDGLVELATICALCNDSSLDFNETKGVYEKVGEATETALTTLVEKMNVFNTEVRNLSKVERANACNSVIRQLMKKEFTLEFSRDRKSMSVYCSPAKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPMTGPVKEKILSVIKEWGTGRDTLRCLALATRDTPPKREEMVLDDSSRFMEYETDLTFVGVVGMLDPPRKEVMGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFGENEEVADRAYTGREFDDLPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRSPKEPLISGWLFFRYMAIGGYVGAATVGAAAWWFMYAEDGPGVTYHQLTHFMQCTEDHPHFEGLDCEIFEAPEPMTMALSVLVTIEMCNALNSLSENQSLMRMPPWVNIWLLGSICLSMSLHFLILYVDPLPMIFKLKALDLTQWLMVLKISLPVIGLDEILKFIARNYLEDPEDERRK	P04191 UniProt Entry: ATA1_RABIT UniProt Gene: ATP2A1 UniProt Name: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 PIR Number: PWRBFC	1SU4 PDB Title: Calcium-Transporting ATPase Sarcoplasmic Reticulum Type, Fast Twitch Skeletal Muscle, Adult Isoform, Chain A	Toyoshima et al. (2000). Toyoshima C, Nakasako M, Nomura H, & Ogawa H (2000). Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405 :647-655. PubMed Id: 10864315.
*phospholamban pentamer: Homo sapiens* E Eukaryota** Sequence from PDB. Sequence is for one monomer in pentamer. Also see 1FJK, 1FJP (cardiac phospholamban from pig) N Terminal: in TM Segment Count: 1 TM Segments: A.23,52; Sequence: MEKVQYLTRSAIRRASTIEMPQQARQKLQNLFINFCLILICLLLICIIVMLL	PPLA_HUMAN UniProt Entry: P26678 UniProt Gene: PLN UniProt Name: Cardiac phospholamban PIR Number: A40424	1ZLL PDB Title: NMR Structure of Unphosphorylated Human Phospholamban Pentamer	Oxenoid and Chou (2005). Oxenoid K & Chou JJ (2005). The structure of phospholamban pentamer reveals a channel-like architecture in membranes. Proc Natl Acad Sci USA 102 :10870-10875. PubMed Id: 16043693.
Type IX Secretion System Motors These are α-helical proteins that power secretion of adhesin proteins. See Type IX Secretion System in β-barrel Proteins.
Decarboxylases
Hydrolases
Oxygenases
*Metalloenzyme pMMO subunit pmoA: Methylococcus capsulatus* B Bacteria** Homotrimer. Sequence for monomer from Swiss-Prot. This corresponds to chain B in PDB file. 2 TM segments, F and G are not a full TM helices. TM segment F is probably not a helix and TM segment G is only a partial helix. N Terminal: in TM Segment Count: 7 TM Segments: A.11,43; B.59,79; C.88,105; D.125,136; E.141,167; F.193,216; G.220,242; Sequence: MSAAQSAVRSHAEAVQVSRTIDWMALFVVFFVIVGSYHIHAMLTMGDWDFWSDWKDRRLWVTVTPIVLVTFPAAVQSYLWERYRLPWGATVCVLGLLLGEWINRYFNFWGWTYFPINFVFPASLVPGAIILDTVLMLSGSYLFTAIVGAMGWGLIFYPGNWPIIAPLHVPVEYNGMLMSIADIQGYNYVRTGTPEYIRMVEKGTLRTFGKDVAPVSAFFSAFMSILIYFMWHFIGRWFSNERFLQST	Q607G3 UniProt Entry: Q607G3_METCA UniProt Gene: pmoA UniProt Name: Methane monooxygenase, A subunit PIR Number:	1YEW PDB Title: Crystal structure of particulate methane monooxygenase	Lieberman & Rosenzweig (2005). Lieberman RL & Rosenzweig AC (2005). Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature 434 :177-181. PubMed Id: 15674245.
*Metalloenzyme pMMO subunit pmoB: Methylococcus capsulatus* B Bacteria** Homotrimer. Sequence for monomer from Swiss-Prot. This corresponds to chain A in PDB file. N Terminal: out TM Segment Count: 2 TM Segments: A.185,207; B.232,256; Sequence: MKTIKDRIAKWSAIGLLSAVAATAFYAPSASAHGEKSQAAFMRMRTIHWYDLSWSKEKVKINETVEIKGKFHVFEGWPETVDEPDVAFLNVGMPGPVFIRKESYIGGQLVPRSVRLEIGKTYDFRVVLKARRPGDWHVHTMMNVQGGGPIIGPGKWITVEGSMSEFRNPVTTLTGQTVDLENYNEGNTYFWHAFWFAIGVAWIGYWSRRPIFIPRLLMVDAGRADELVSATDRKVAMGFLAATILIVVMAMSSANSKYPITIPLQAGTMRGMKPLELPAPTVSVKVEDATYRVPGRAMRMKLTITNHGNSPIRLGEFYTASVRFLDSDVYKDTTGYPEDLLAEDGLSVSDNSPLAPGETRTVDVTASDAAWEVYRLSDIIYDPDSRFAGLLFFFDATGNRQVVQIDAPLIPSFM	Q49104 UniProt Entry: Q49104_METCA UniProt Gene: pmoB UniProt Name: Particulate methane monooxygenase 45 kDa subunit [Precursor] PIR Number: B57266	1YEW PDB Title: Crystal structure of particulate methane monooxygenase	Lieberman & Rosenzweig (2005). Lieberman RL & Rosenzweig AC (2005). Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature 434 :177-181. PubMed Id: 15674245.
*Metalloenzyme pMMO subunit pmoC: Methylococcus capsulatus* B Bacteria** Homotrimer. Sequence for monomer from Swiss-Prot. This corresponds to chain C in PDB file. N Terminal: in TM Segment Count: 5 TM Segments: A.51,76; B.90,113; C.126,149; D.171,198; E.202,249; Sequence: MHETKQGGEKRFTGAICRCSHRYNSMEVKMAATTIGGAAAAEAPLLDKKWLTFALAIYTVFYLWVRWYEGVYGWSAGLDSFAPEFETYWMNFLYTEIVLEIVTASILWGYLWKTRDRNLAALTPREELRRNFTHLVWLVAYAWAIYWGASYFTEQDGTWHQTIVRDTDFTPSHIIEFYLSYPIYIITGFAAFIYAKTRLPFFAKGISLPYLVLVVGPFMILPNVGLNEWGHTFWFMEELFVAPLHYGFVIFGWLALAVMGTLTQTFYSFAQGGLGQSLCEAVDEGLIAK	O05111 UniProt Entry: O05111_METCA UniProt Gene: pmoC2 UniProt Name: Methane monooxygenase subunit C2 PIR Number:	1YEW PDB Title: Crystal structure of particulate methane monooxygenase	Lieberman & Rosenzweig (2005). Lieberman RL & Rosenzweig AC (2005). Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature 434 :177-181. PubMed Id: 15674245.
Transhydrogenases
Mo/Wbis-MGD Oxidoreductases
Oxidoreductases
*nitrate reductase A, NarI membrane anchor: Escherichia coli* B Bacteria** Sequence from Swiss-Prot. TMhelices=5. N Terminal: out TM Segment Count: 5 TM Segments: A.2,28; B.49,72; C.82,119; D.122,149; E.182,200; Sequence: MQFLNMFFFDIYPYIAGAVFLIGSWLRYDYGQYTWRAASSQMLDRKGMNLASNLFHIGILGIFVGHFFGMLTPHWMYEAWLPIEVKQKMAMFAGGASGVLCLIGGVLLLKRRLFSPRVRATTTGADILILSLLVIQCALGLLTIPFSAQHMDGSEMMKLVGWAQSVVTFHGGASQHLDGVAFIFRLHLVLGMTLFLLFPFSRLIHIWSVPVEYLTRKYQLVRARH	P11350 UniProt Entry: NARI_ECOLI UniProt Gene: NARI, CHLI, B1227 UniProt Name: Respiratory nitrate reductase 1 gamma chain PIR Number: C27737, RDECNG	1Q16 PDB Title: Respiratory Nitrate Reductase 1 gamma Chain	Bertero et al. (2003). Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, & Strynadka NC (2003). Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nature Structural Biol 10 :681-687. PubMed Id: 12910261.
*NrfH: Desulfovibrio vulgaris* B Bacteria** Sequence from PDB, chain C. N Terminal: in TM Segment Count: 1 TM Segments: A.14,38; Sequence: MSEEKSRNGPARLKLVLGGATLGVVALATVAFGMKYTDQRPFCTSCHIMNPVGVTHKLSGHANISCNDCHAPHNLLAKLPFKAIAGARDVYMNTLGHPGDLILAGMETKEVVNANCKACHTMTNVEVASMEAKKYCTDCHRNVQHMRMKPISTREVADE		2J7A PDB Title: CRYSTAL STRUCTURE OF CYTOCHROME C NITRITE REDUCTASE NRFHA COMPLEX FROM DESULFOVIBRIO VULGARIS	Rodrigues et al. (2006). Rodrigues ML, Oliveira TF, Pereira AC & Archer M (2006). X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination. EMBO J 25 :5951-5960. PubMed Id: 17139260.
*Cysteine Oxidase DsbB: Escherichia coli* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain B in PDB file. N Terminal: in TM Segment Count: 4 TM Segments: A.15,36; B.46,65; C.72,93; D.145,163; Sequence: MLRFLNQCSQGRGAWLLMAFTALALELTALWFQHVMLLKPCVLCIYERCALFGVLGAALIGAIAPKTPLRYVAMVIWLYSAFRGVQLTYEHTMLQLYPSPFATCDFMVRFPEWLPLDKWVPQVFVASGDCAERQWDFLGLEMPQWLLGIFIAYLIVAVLVVISQPFKAKKRDLFGR	P0A6M2 UniProt Entry: DSBB_ECOLI UniProt Gene: dsbB UniProt Name: Disulfide bond formation protein B PIR Number: F64864	2HI7 PDB Title: Crystal structure of DsbA-DsbB-ubiquinone complex	Inaba et al. (2006). Inaba K, Murakami S, Suzuki M, Nakagawa A, Yamashita E, Okada K, & Ito K (2006). Crystal structure of the DsbA-DsbB complex reveals a mechanism of disulfide bond generation. Cell 127 :789-801. PubMed Id: 17110337.
Heme-Handling Proteins
Electron Transport Chain Complexes: Complex I
Electron Transport Chain Complexes: Complex II
*Fumarate Reductase. 15 kD anchor: Escherichia coli* B Bacteria** Chain C in PDB file. Helix A and B connected by very short turns to an interfacial helix (N51-L63). Nterm in = cytoplasm. Sequence from Swiss-Prot. TMhelices=3. N Terminal: in TM Segment Count: 3 TM Segments: A.22,49; B.66,90; C.105,128; Sequence: MTTKRKPYVRPMTSTWWKKLPFYRFYMLREGTAVPAVWFSIELIFGLFALKNGPEAWAGFVDFLQNPVIVIINLITLAAALLHTKTWFELAPKAANIIVKDEKMGPEPIIKSLWAVTVVATIVILFVALYW	P03805 UniProt Entry: FRDC_ECOLI UniProt Gene: FRDC, B4152, C5240, Z5759, ECS5133 UniProt Name: Fumarate reductase 15 kDa hydrophobic protein PIR Number: S56380	1FUM PDB Title: fumarate reductase 15 kD hydrophobic protein, Chain C	Iverson et al. (1999). Iverson TM, Luna-Chavez C, Cecchini G, & Rees DC (1999). Structure of the Escherichia coli fumerate reductase respiratory complex. Science 284 :1961-1966. PubMed Id: 10373108.
*Fumarate Reductase. 13 kD anchor: Escherichia coli* B Bacteria** Chain D in PDB file. Helix A strongly (strangely!) kinked at about Ile26. Nterm in = cytoplasm. Sequence from Swiss-Prot. TMhelices=3. N Terminal: in TM Segment Count: 3 TM Segments: A.9,35; B.61,89; C.97,115; Sequence: MINPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGDALSYERVLAFAQSFIGRVFLFLMIVLPLWCGLHRMHHAMHDLKIHVPAGKWVFYGLAAILTVVTLIGVVTI	P03806 UniProt Entry: FRDD_ECOLI UniProt Gene: FRDD, B4151, Z5758, ECS5132, SF4309 UniProt Name: Fumarate reductase 13 kDa hydrophobic protein PIR Number: WMEC13	1L0V PDB Title: Fumarate Reductase 13 Kda Hydrophobic Protein	Iverson et al. (1999). Iverson TM, Luna-Chavez C, Cecchini G, & Rees DC (1999). Structure of the Escherichia coli fumerate reductase respiratory complex. Science 284 :1961-1966. PubMed Id: 10373108.
*Fumarate Reductase alpha subunit: Wolinella succinogenes* B Bacteria** Chain C in PDB file. Nterm in = cytoplasm. Sequence from Swiss-Prot. TMhelices=5. N Terminal: in TM Segment Count: 5 TM Segments: A.22,52; B.77,100; C.121,149; D.169,194; E.202,237; Sequence: MTNESILESYSGVTPERKKSRMPAKLDWWQSATGLFLGLFMIGHMFFVSTILLGDNVMLWVTKKFELDFIFEGGKPIVVSFLAAFVFAVFIAHAFLAMRKFPINYRQYLTFKTHKDLMRHGDTTLWWIQAMTGFAMFFLGSVHLYIMMTQPQTIGPVSSSFRMVSEWMWPLYLVLLFAVELHGSVGLYRLAVKWGWFDGETPDKTRANLKKLKTLMSAFLIVLGLLTFGAYVKKGLEQTDPNIDYKYFDYKRTHHR	P17413 UniProt Entry: FRDC_WOLSU UniProt Gene: FRDC UniProt Name: Fumarate reductase cytochrome B subunit PIR Number: S10164	2BS2 PDB Title: Fumarate Reductase Cytochrome B Subunit, Chain C, F. Other details - Haem Axial Ligands - His 44, His 93, His 143, His 182	Lancaster et al. (1999). Lancaster CRD, Kröger A, Auer M, & Michel H (1999). Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution. Nature 402 :377-385. PubMed Id: 10586875.
*formate dehydrogenase-N, beta chain: Escherichia coli* B Bacteria** Chain B in PDB. Sequence from Swiss-Prot. TMhelices=1. N Terminal: out TM Segment Count: 1 TM Segments: A.248,280; Sequence: MAMETQDIIKRSATNSITPPSQVRDYKAEVAKLIDVSTCIGCKACQVACSEWNDIRDEVGHCVGVYDNPADLSAKSWTVMRFSETEQNGKLEWLIRKDGCMHCEDPGCLKACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFNIPRLNKEDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIHFGTKKEMLELAEQRVAKLKARGYEHAGVYNPEGVGGTHVMYVLHHADQPELYHGLPKDPKIDTSVSLWKGALKPLAAAGFIATFAGLIFHYIGIGPNKEVDDDEEDHHE	P24184 UniProt Entry: FDNH_ECOLI UniProt Gene: FDNH, B1475, SF1750 UniProt Name: Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit PIR Number: JS0629	1KQF 1KQG PDB Title: formate dehydrogenase, nitrate-inducible, major subunit	Jormakka et al. (2002). Jormakka M, Tornroth S, Byrne B, & Iwata S (2002). Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295 :1863-1868. PubMed Id: 11884747.
*formate dehydrogenase-N, gamma chain: Escherichia coli* B Bacteria** Chain C in PDB. Sequence from Swiss-Prot. TMhelices=4. N Terminal: in TM Segment Count: 4 TM Segments: A.15,37; B.51,74; C.112,134; D.146,175; Sequence: MSKSKMIVRTKFIDRACHWTVVICFFLVALSGISFFFPTLQWLTQTFGTPQMGRILHPFFGIAIFVALMFMFVRFVHHNIPDKKDIPWLLNIVEVLKGNEHKVADVGKYNAGQKMMFWSIMSMIFVLLVTGVIIWRPYFAQYFPMQVVRYSLLIHAAAGIILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYREIEKAEAKKESEEGI	P24185 UniProt Entry: FDNI_ECOLI UniProt Gene: FDNI, B1476, Z2234, ECS2080, SF1749 UniProt Name: Formate dehydrogenase, nitrate-inducible, cytochrome b556(FDN) subunit PIR Number: JS0630	1KQG 1KQF PDB Title: formate dehydrogenase, nitrate-inducible, major subunit	Jormakka et al. (2002). Jormakka M, Tornroth S, Byrne B, & Iwata S (2002). Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295 :1863-1868. PubMed Id: 11884747.
*succinate dehydrogenase C subunit: Escherichia coli* B Bacteria** Sequence is from Swiss-Prot. TMhelices=3. N Terminal: in TM Segment Count: 3 TM Segments: A.21,51; B.67,96; C.102,128; Sequence: MIRNVKKQRPVNLDLQTIRFPITAIASILHRVSGVITFVAVGILLWLLGTSLSSPEGFEQASAIMGSFFVKFIMWGILTALAYHVVVGIRHMMMDFGYLEETFEAGKRSAKISFVITVVLSLLAGVLVW	P10446 UniProt Entry: DHSC_ECOLI UniProt Gene: SDHC, CYBA, B0721, Z0875, ECS0746 UniProt Name: Succinate dehydrogenase cytochrome b-556 subunit PIR Number:	1NEK PDB Title: Succinate Dehydrogenase Cytochrome B-556 Subunit	Yankovskaya et al. (2003). Yankovskaya V, Horsefield R, Törnroth S, Luna-Chavez C, Miyoshi H, Léger C, Byrne B, Cecchini G, & Iwata S (2003). Architecture of succinate dehydrogenase and reactive oxygen species generation. Science 299 :700-704. PubMed Id: 12560550.
*succinate dehydrogenase D subunit: Escherichia coli* B Bacteria** Sequence is from Swiss-Prot. TMhelices=3. N Terminal: in TM Segment Count: 3 TM Segments: A.11,36; B.53,81; C.86,113; Sequence: MVSNASALGRNGVHDFILVRATAIVLTLYIIYMVGFFATSGELTYEVWIGFFASAFTKVFTLLALFSILIHAWIGMWQVLTDYVKPLALRLMLQLVIVVALVVYVIYGFVVVWGV	P10445 UniProt Entry: DHSD_ECOLI UniProt Gene: SDHD, B0722, C0800, SF0575 UniProt Name: Succinate dehydrogenase hydrophobic membrane anchor protein PIR Number:	1NEK PDB Title: Succinate Dehydrogenase Hydrophobic Membrane Anchor Protein	Yankovskaya et al. (2003). Yankovskaya V, Horsefield R, Törnroth S, Luna-Chavez C, Miyoshi H, Léger C, Byrne B, Cecchini G, & Iwata S (2003). Architecture of succinate dehydrogenase and reactive oxygen species generation. Science 299 :700-704. PubMed Id: 12560550.
*Mito. Respiratory Complex protein CybL: Sus scrofa (Pig)* E Eukaryota** Sequence from PDB,chain C. PDB sequence starts from res#4. Assigned TM segments account for this. TM helices correspond to 2L,4L and 5L in the article. No Swiss-Prot file for this protein. Matrix=in. N Terminal: in TM Segment Count: 3 TM Segments: A.34,62; B.81,109; C.116,137; Sequence: LGTTAKEEMERFWNKNLGSNRPLSPHITIYRWSLPMAMSICHRGTGIALSAGVSLFGLSALLLPGNFESHLELVKSLCLGPTLIYTAKFGIVFPLMYHTWNGIRHLIWDLGKGLTIPQLTQSGVVVLILTVLSSVGLAAM		1ZOY PDB Title: Crystal Structure of Mitochondrial Respiratory Complex II from porcine heart at 2.4 Angstroms	Sun et al. (2005). Sun F, Huo X, Zhai Y, Wang A, Xu J, Su D, Bartlam M, & Rao Z (2005). Crystal structure of mitochondrial respiratory membrane protein complex II. Cell 121 :1043-1057. PubMed Id: 15989954.
*Mito. Respiratory protein CybS: Sus scrofa (Pig)* E Eukaryota** Sequence from PDB, chain D. PDB sequence starts with res#34. Assigned TM segments account for this. TM helices correspond to 1S,2S and 3S in the article. No Swiss-Prot file for this protein. Matrix=in. N Terminal: in TM Segment Count: 3 TM Segments: A.4,29; B.34,58; C.65,88; Sequence: ASSKAASLHWTGERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGIGQVVTDYVRGDALQKAAKAGLLALSAFTFAGLCYFNYHDVGICKAVAMLWKL		1ZOY PDB Title: Crystal Structure of Mitochondrial Respiratory Complex II from porcine heart at 2.4 Angstroms	Sun et al. (2005). Sun F, Huo X, Zhai Y, Wang A, Xu J, Su D, Bartlam M, & Rao Z (2005). Crystal structure of mitochondrial respiratory membrane protein complex II. Cell 121 :1043-1057. PubMed Id: 15989954.
Electron Transport Chain Complexes: Complex III (Cytochrome bc₁) Information about Cytochrome bc₁
*cyto. bc1 complex. Chain C: Bos taurus (Bovine)* E Eukaryota** Chain designation is that of PDB. Corresponds to cytochrome b in cited paper. Matrix = in. TMhelices=8. N Terminal: in TM Segment Count: 8 TM Segments: A.29,53; B.76,104; C.110,133; D.172,202; E.224,245; F.287,307; G.319,340; H.345,376; Sequence: MTNIRKSHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTFLETWNIGVILLLTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIIMAIAMVHLLFLHETGSNNPTGISSDVDKIPFHPYYTIKDILGALLLILALMLLVLFAPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAFSILILALIPLLHTSKQRSMMFRPLSQCLFWALVADLLTLTWIGGQPVEHPYITIGQLASVLYFLLILVLMPTAGTIENKLLKW	P00157 UniProt Entry: CYB_BOVIN UniProt Gene: MTCYB, COB, CYTB UniProt Name: Cytochrome b PIR Number: CBBO	1BGY 1QCR 1BCC PDB Title: Cytochrome Bc1 Complex from Bovine	Iwata et al. (1998). Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, Link TA, Ramaswamy S, & Jap BK (1998). Complete structure of the 11-subunit bovine mitochondrial cytochrome bc₁complex. Science 281 :64-71. PubMed Id: 9651245.
*cyto. bc1 complex. Chain D: Bos taurus (Bovine)* E Eukaryota** Chain designation is that of PDB. Corresponds to cytochrome C1 in cited paper. Matrix = in. TMhelices=1. N Terminal: out TM Segment Count: 1 TM Segments: A.197,232; Sequence: SDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCSSCHSMDYVAYRHLVGVCYTEDEAKALAEEVEVQDGPNEDGEMFMRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIGMAPPIYNEVLEFDDGTPATMSQVAKDVCTFLRWAAEPEHDHRKRMGLKMLLMMGLLLPLVYAMKRHKWSVLKSRKLAYRPPK	P00125 UniProt Entry: CY1_BOVIN UniProt Gene: CYC1 UniProt Name: Cytochrome c1, heme protein, mitochondrial PIR Number: CCBO1	1BGY 1QCR 1BCC PDB Title: Cytochrome Bc1 Complex from Bovine	Iwata et al. (1998). Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, Link TA, Ramaswamy S, & Jap BK (1998). Complete structure of the 11-subunit bovine mitochondrial cytochrome bc₁complex. Science 281 :64-71. PubMed Id: 9651245.
*cyto. bc1 complex. Chain G: Bos taurus (Bovine)* E Eukaryota** Chain designation is that of PDB. Corresponds to subunit 7 of cited reference. Sequence also from PDB file. PIR sequence differs in one position from the PDB and Swiss-Prot sequence. Matrix = in. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.29,71; Sequence: GRQFGHLTRVRHLITYSLSPFEQRPFPHYFSKGVPNVWRRLRACILRVAPPFLAFYLLYTWGTQEFEKSKRKNPAAYVNDR	P13271 UniProt Entry: UCRQ_BOVIN UniProt Gene: UniProt Name: Ubiquinol-cytochrome C reductase complex ubiquinone-binding protein QP-C PIR Number: A24864	1BGY 1QCR 1BCC PDB Title: Cytochrome Bc1 Complex from Bovine - chain G	Iwata et al. (1998). Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, Link TA, Ramaswamy S, & Jap BK (1998). Complete structure of the 11-subunit bovine mitochondrial cytochrome bc₁complex. Science 281 :64-71. PubMed Id: 9651245.
*cyto. bc1 complex. Chain J: Bos taurus (Bovine)* E Eukaryota** Chain designation is that of PDB. Corresponds to subunit 10 in cited paper. Sequence also from PDB file. PIR sequence equal in length but differs in one residue. Matrix = in. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.17,48; Sequence: VAPTLTARLYSLLFRRTSTFALTIVVGALLFERAFDQGADAIYEHINEGKLWKHIKHKYENK	P00130 UniProt Entry: UCRX_BOVIN UniProt Gene: UniProt Name: Ubiquinol-cytochrome C reductase complex 7.2 kDa protein PIR Number: CCBO17	1BGY 1QCR 1BCC PDB Title: Cytochrome Bc1 Complex from Bovine	Iwata et al. (1998). Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, Link TA, Ramaswamy S, & Jap BK (1998). Complete structure of the 11-subunit bovine mitochondrial cytochrome bc₁complex. Science 281 :64-71. PubMed Id: 9651245.
*cyto. bc1 complex. Chain K: Bos taurus (Bovine)* E Eukaryota** Chain designation is that of PDB. Corresponds to subunit II in cited paper. Sequence also from PDB file. PDB and PIR are identical, but the Swiss-Prot sequence differs in 3 positions, 2 in the TM domain. Matrix = in. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.17,35; Sequence: MLTRFLGPRYRQLARNWVPTAQLWGAVGAVGLVSATDSRLILDWVPYINGKFKKDD	P07552 UniProt Entry: UCRY_BOVIN UniProt Gene: UniProt Name: Ubiquinol-cytochrome C reductase complex 6.4 kDa protein PIR Number: CBBOC6	1BGY 1QCR 1BCC PDB Title: Cytochrome Bc1 Complex from Bovine	Iwata et al. (1998). Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, Link TA, Ramaswamy S, & Jap BK (1998). Complete structure of the 11-subunit bovine mitochondrial cytochrome bc₁complex. Science 281 :64-71. PubMed Id: 9651245.
*cyto. bc1 complex. Chain E: Bos taurus (Bovine)* E Eukaryota** Chain designation is that of PDB. Sequence from PDB, which is highly truncated, at both ends, relative to Swiss-Prot. Corresponds to Rieske protein TM domain. Matrix = in. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.31,61; Sequence: SHTDIKVPDFSDYRRPEVLDSTKSSKESSEARKGFSYLVTATTTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDPQHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG	P13272 UniProt Entry: UCRI_BOVIN UniProt Gene: UQCRFS1 UniProt Name: Ubiquinol-cytochrome C reductase iron-sulfur subunit, mitochondrial [Precursor] PIR Number: A34660	1BGY 1QCR 1BCC PDB Title: Cytochrome Bc1 Complex from Bovine	Iwata et al. (1998). Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, Link TA, Ramaswamy S, & Jap BK (1998). Complete structure of the 11-subunit bovine mitochondrial cytochrome bc₁complex. Science 281 :64-71. PubMed Id: 9651245.
Electron Transport Chain Complexes: Cytochrome b₆f of Oxygenic Photosynthesis
*cyt. b6f complex, cyto b6 subunit: Mastigocladus laminosus* B Bacteria** Sequence is from PDB. Thylakoid lumen is defined as 'in'. TMhelices=4. N Terminal: out TM Segment Count: 4 TM Segments: A.34,55; B.79,109; C.116,137; D.178,205; Sequence: MANVYDWFQERLEIQALADDVTSKYVPPHVNIFYCLGGITLTCFLIQFATGFAMTFYYKPTVTEAYASVQYIMNEVSFGWLIRSIHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWISGVILAVITVSFGVTGYSLPWDQVGYWAVKIVSGVPEAIPVVGVLISDLLRGGSSVGQATLTRYYSAHTFVLPWLIAVFMLLHFLMIRKQGISGPL		1VF5 PDB Title: Cytochrome B6, Chain A	Kurisu et al. (2003). Kurisu G, Zhang H, Smith JL, & Cramer WA (2003). Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302 :1009-1014. PubMed Id: 14526088.
*cyt. b6f complex, subunit IV: Mastigocladus laminosus* B Bacteria** Sequence is from PDB. Thylakoid lumen is defined as 'in'. TMhelices=3. N Terminal: out TM Segment Count: 3 TM Segments: A.35,59; B.97,115; C.127,145; Sequence: MATLKKPDLSDPKLRAKLAKGMGHNYYGEPAWPNDLLYVFPVVIMGTFACIVALSVLDPAMVGEPANPFATPLEILPEWYLYPVFQILRSLPNKLLGVLLMASVPLGLILVPFIENVNKFQNPFRRPVATTIFLFGTLVTIWLGIGAALPLDKTLTLGLF		1VF5 PDB Title: Subunit IV, chain B	Kurisu et al. (2003). Kurisu G, Zhang H, Smith JL, & Cramer WA (2003). Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302 :1009-1014. PubMed Id: 14526088.
*cyt. b6f complex, cytochrome f: Mastigocladus laminosus* B Bacteria** Sequence is from PDB. Thylakoid lumen is defined as 'in'. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.252,279; Sequence: YPFWAQQTYPPTPREPTGRIVCANCHLAAKPAEVEVPQSVLPDTVFKAVVKIPYDTKLQQVAADGSKVGLNVGAVLMLPEGFKIAPEERIPEELKKEVGDVYFQPYKEGQDNVLLVGPLPGEQYQEIVFPVLSPNPTTDKNIHFGKYAIHLGANRGRGQIYPTGEKSNNNVFTASATGTITKIAKEEDEYGNVKYQVSIQTDSGKTVVDTIPAGPELIVSEGQAVKAGEALTNNPNVGGFGQDDTEIVLQDPNRVKWMIAFICLVMLAQLMLILKKKQVEKVQAAEMNF		1VF5 PDB Title: cytochrome f, chain C	Kurisu et al. (2003). Kurisu G, Zhang H, Smith JL, & Cramer WA (2003). Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302 :1009-1014. PubMed Id: 14526088.
*cyt. b6f complex, Rieske iron-sulfur protein: Mastigocladus laminosus* B Bacteria** Sequence is from PDB. Thylakoid lumen is defined as 'in'. TMhelices=1. N Terminal: out TM Segment Count: 1 TM Segments: A.19,43; Sequence: MAQFTESMDVPDMGRRQFMNLLAFGTVTGVALGALYPLVKYFIPPSGGAVGGGTTAKDKLGNNVKVSKFLESHNAGDRVLVQGLKGDPTYIVVESKEAIRDYGINAVCTHLGCVVPWNAAENKFKCPCHGSQYDETGRVIRGPAPLSLALCHATVQDDNIVLTPWTETDFRTGEKPWWV		1VF5 PDB Title: Rieske iron-sulfur protein, chain D	Kurisu et al. (2003). Kurisu G, Zhang H, Smith JL, & Cramer WA (2003). Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302 :1009-1014. PubMed Id: 14526088.
*cyt. b6f complex, PetL: Mastigocladus laminosus* B Bacteria** Sequence is from PDB. Thylakoid lumen is defined as 'in'. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.1,25; Sequence: MILGAVFYIVFIALFFGIAVGIIFAIKSIKLI		1VF5 PDB Title: Pet L, chain E	Kurisu et al. (2003). Kurisu G, Zhang H, Smith JL, & Cramer WA (2003). Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302 :1009-1014. PubMed Id: 14526088.
*cyt. b6f complex, PetM: Mastigocladus laminosus* B Bacteria** Sequence is from PDB. Thylakoid lumen is defined as 'in'. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.2,30; Sequence: MTEEMLYAALLSFGLIFVGWGLGVLLLKIQGAEKE		1VF5 PDB Title: Pet M, chain F	Kurisu et al. (2003). Kurisu G, Zhang H, Smith JL, & Cramer WA (2003). Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302 :1009-1014. PubMed Id: 14526088.
*cyt. b6f complex, PetG: Mastigocladus laminosus* B Bacteria** Sequence is from PDB. Thylakoid lumen is defined as 'in'. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.9,31; Sequence: MVEPLLDGLVLGLVFATLGGLFYAAYQQYKRPNELGG		1VF5 PDB Title: Pet G, Chain G	Kurisu et al. (2003). Kurisu G, Zhang H, Smith JL, & Cramer WA (2003). Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302 :1009-1014. PubMed Id: 14526088.
*cyt. b6f complex, PetN: Mastigocladus laminosus* B Bacteria** Sequence is from PDB. Thylakoid lumen is defined as 'in'. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.3,29; Sequence: MEIDVLGWVALLVVFTWSIAMVVWGRNGL		1VF5 PDB Title: Pet N, chain H	Kurisu et al. (2003). Kurisu G, Zhang H, Smith JL, & Cramer WA (2003). Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302 :1009-1014. PubMed Id: 14526088.
Electron Transport Chain Complexes: Complex IV (Cytochrome C Oxidase) ( Information about cytochrome c oxidases)
*cyto. C oxidase. Subunit I: Bos taurus (Bovine)* E Eukaryota** Chain A in PDB file. Nterm in = matrix. Sequence from Swiss-Prot. TMhelices=12. N Terminal: in TM Segment Count: 12 TM Segments: A.12,40; B.51,86; C.95,117; D.141,170; E.183,212; F.238,261; G.270,286; H.299,327; I.336,357; J.371,400; K.407,433; L.447,478; Sequence: MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFAIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTMWNTISSMGSFISLTAVMLMVFIIWEAFASKREVLTVDLTTTNLEWLNGCPPPYHTFEEPTYVNLK	P00396 UniProt Entry: COX1_BOVIN UniProt Gene: MTCO1, COI UniProt Name: Cytochrome c oxidase polypeptide I PIR Number: ODBO1	1OCC PDB Title: cytochrome c oxidase	Tsukihara et al. (1996). Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, & Yoshikawa S (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 :1136-1144. PubMed Id: 8638158.
*cyto. C oxidase. Subunit II: Bos taurus (Bovine)* E Eukaryota** Chain B in PDB file. Nterm in = matrix. Sequence from Swiss-Prot. TMhelices=2. N Terminal: out TM Segment Count: 2 TM Segments: A.15,45; B.60,87; Sequence: MAYPMQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSELKPGELRLLEVDNRVVLPMEMTIRMLVSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSSRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML	P00404 UniProt Entry: COX2_BOVIN UniProt Gene: MTCO2, COII UniProt Name: Cytochrome c oxidase polypeptide II PIR Number: OBBO2	1OCC PDB Title: cytochrome c oxidase	Tsukihara et al. (1996). Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, & Yoshikawa S (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 :1136-1144. PubMed Id: 8638158.
*cyto. C oxidase. Subunit III: Bos taurus (Bovine)* E Eukaryota** Chain C in PDB file. Nterm in = matrix. Sequence from Swiss-Prot. TMhelices=7. N Terminal: in TM Segment Count: 7 TM Segments: A.16,34; B.41,66; C.73,105; D.129,152; E.156,183; F.191,223; G.233,256; Sequence: MTHQTHAYHMVNPSPWPLTGALSALLMTSGLTMWFHFNSMTLLMIGLTTNMLTMYQWWRDVIRESTFQGHHTPAVQKGLRYGMILFIISEVLFFTGFFWAFYHSSLAPTPELGGCWPPTGIHPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGDRKHMLQALFITITLGVYFTLLQASEYYEAPFTISDGVYGSTFFVATGFHGLHVIIGSTFLIVCFFRQLKFHFTSNHHFGFEAGAWYWHFVDVVWLFLYVSIYWWGS	P00415 UniProt Entry: COX3_BOVIN UniProt Gene: MTCO3, COIII UniProt Name: Cytochrome c oxidase polypeptide III PIR Number: OTBO3	1OCC PDB Title: cytochrome c oxidase	Tsukihara et al. (1996). Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, & Yoshikawa S (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 :1136-1144. PubMed Id: 8638158.
*cyto. C oxidase. Subunit IV: Bos taurus (Bovine)* E Eukaryota** Chain D in PDB file. Nterm in = matrix. Sequence is processed sequence from Swiss-Prot (22 AA signal sequence removed). TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.77,103; Sequence: AHGSVVKSEDYALPSYVDRRDYPLPDVAHVKNLSASQKALKEKEKASWSSLSIDEKVELYRLKFKESFAEMNRSTNEWKTVVGAAMFFIGFTALLLIWEKHYVYGPIPHTFEEEWVAKQTKRMLDMKVAPIQGFSAKWDYDKNEWKK	P00423 UniProt Entry: CX41_BOVIN UniProt Gene: COX4I1, COX4 UniProt Name: Cytochrome c oxidase subunit IV isoform 1, mitochondrial [Precursor] PIR Number: OLBO4	1OCC PDB Title: cytochrome c oxidase	Tsukihara et al. (1996). Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, & Yoshikawa S (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 :1136-1144. PubMed Id: 8638158.
*cyto. C oxidase. Subunit VIa: Bos taurus (Bovine)* E Eukaryota** Chain G in PDB file. Nterm in = matrix. Nterm buried within membrane. Nterm end of helix is 'in'. Sequence is processed sequence from Swiss-Prot (12 AA signal sequence removed). TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.13,37; Sequence: ASAAKGDHGGTGARTWRFLTFGLALPSVALCTLNSWLHSGHRERPAFIPYHHLRIRTKPFSWGDGNHTFFHNPRVNPLPTGYEKP	P07471 UniProt Entry: CX6A2_BOVIN UniProt Gene: COX6A2, COX6A UniProt Name: Cytochrome c oxidase polypeptide VIa-heart, mitochondrial [Precursor] PIR Number: OGBO6	1OCC PDB Title: cytochrome c oxidase	Tsukihara et al. (1996). Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, & Yoshikawa S (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 :1136-1144. PubMed Id: 8638158.
*cyto. C oxidase. Subunit VIc: Bos taurus (Bovine)* E Eukaryota** Chain I in PDB file. Nterm in = matrix. Sequence from Swiss-Prot. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.12,52; Sequence: STALAKPQMRGLLARRLRFHIVGAFMVSLGFATFYKFAVAEKRKKAYADFYRNYDSMKDFEEMRKAGIFQSAK	P04038 UniProt Entry: COXH_BOVIN UniProt Gene: COX6C UniProt Name: Cytochrome c oxidase polypeptide VIc PIR Number: OGBO6C	1OCC PDB Title: cytochrome c oxidase	Tsukihara et al. (1996). Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, & Yoshikawa S (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 :1136-1144. PubMed Id: 8638158.
*cyto. C oxidase. Subunit VIIa: Bos taurus (Bovine)* E Eukaryota** Chain J in PDB file. Nterm in = matrix. Sequence is processed sequence from Swiss-Prot (21 AA signal sequence removed). TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.26,54; Sequence: FENRVAEKQKLFQEDNGLPVHLKGGATDNILYRVTMTLCLGGTLYSLYCLGWASFPHKK	P07470 UniProt Entry: COXK_BOVIN UniProt Gene: COX7A1, COX7AH, COX7A UniProt Name: Cytochrome c oxidase polypeptide VIIa-heart, mitochondrial [Precursor] PIR Number: OSBO7A	1OCC PDB Title: cytochrome c oxidase	Tsukihara et al. (1996). Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, & Yoshikawa S (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 :1136-1144. PubMed Id: 8638158.
*cyto C oxidase. Subunit VIIb: Bos taurus (Bovine)* E Eukaryota** Chain K in PDB file. Nterm in = matrix. Sequence is processed sequence from Swiss-Prot (24 AA signal sequence removed). TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.9,35; Sequence: IHQKRAPDFHDKYGNAVLASGATFCVAVWVYMATQIGIEWNPSPVGRVTPKEWREQ	P13183 UniProt Entry: COX7B_BOVIN UniProt Gene: COX7B UniProt Name: Cytochrome c oxidase polypeptide VIIb, mitochondrial [Precursor] PIR Number: OSBO7B	1OCC PDB Title: cytochrome c oxidase	Tsukihara et al. (1996). Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, & Yoshikawa S (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 :1136-1144. PubMed Id: 8638158.
*cyto. C oxidase. Subunit VIIc: Bos taurus (Bovine)* E Eukaryota** Chain L in PDB file. Nterm in = matrix. Sequence is processed sequence from Swiss-Prot (16 AA signal sequence removed). TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.18,44; Sequence: SHYEEGPGKNIPFSVENKWRLLAMMTLFFGSGFAAPFFIVRHQLLKK	P00430 UniProt Entry: COX7C_BOVIN UniProt Gene: COX7C, COX7CP1 UniProt Name: Cytochrome c oxidase polypeptide VIIc, mitochondrial [Precursor] PIR Number: OSBO8A	1OCC PDB Title: cytochrome c oxidase	Tsukihara et al. (1996). Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, & Yoshikawa S (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 :1136-1144. PubMed Id: 8638158.
*cyto. C oxidase. Subunit VIII: Bos taurus (Bovine)* E Eukaryota** Chain M in PDB file. Nterm in = matrix. Sequence is processed sequence from Swiss-Prot (24 AA signal sequence removed). TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.12,36; Sequence: ITAKPARTPTSPKEQAIGLSVTFLSFLLPAGWVLYHLDNYKKSSAA	P10175 UniProt Entry: COXQ_BOVIN UniProt Gene: COX8H UniProt Name: Cytochrome c oxidase polypeptide VIII-heart, mitochondrial [Precursor] PIR Number: OSBO8	1OCC PDB Title: cytochrome c oxidase	Tsukihara et al. (1996). Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, & Yoshikawa S (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 :1136-1144. PubMed Id: 8638158.
*cyto. C oxidase. Subunit I: Paracoccus denitrificans* B Bacteria** Chain A in PDB file. See also J. Biol. Chem. (1999) 274:33296-33299. Sequence from Swiss-Prot. TMhelices=12. N Terminal: in TM Segment Count: 12 TM Segments: A.27,59; B.84,121; C.130,151; D.178,206; E.218,251; F.263,298; G.304,322; H.334,362; I.370,395; J.404,430; K.441,468; L.483,513; Sequence: MADAAVHGHGDHHDTRGFFTRWFMSTNHKDIGILYLFTAGIVGLISVCFTVYMRMELQHPGVQYMCLEGARLIADASAECTPNGHLWNVMITYHGVLMMFFVVIPALFGGFGNYFMPLHIGAPDMAFPRLNNLSYWMYVCGVALGVASLLAPGGNDQMGSGVGWVLYPPLSTTEAGYSMDLAIFAVHVSGASSILGAINIITTFLNMRAPGMTLFKVPLFAWSVFITAWLILLSLPVLAGAITMLLMDRNFGTQFFDPAGGGDPVLYQHILWFFGHPEVYIIILPGFGIISHVISTFAKKPIFGYLPMVLAMAAIGILGFVVWAHHMYTAGMSLTQQAYFMLATMTIAVPTGIKVFSWIATMWGGSIEFKTPMLWAFGFLFLFTVGGVTGVVLSQAPLDRVYHDTYYVVAHFHYVMSLGAVFGIFAGVYYWIGKMSGRQYPEWAGQLHFWMMFIGSNLIFFPQHFLGRQGMPRRYIDYPVEFAYWNNISSIGAYISFASFLFFIGIVFYTLFAGKRVNVPNYWNEHADTLEWTLPSPPPEHTFETLPKREDWDRAHAH	P98002 UniProt Entry: CX1B_PARDE UniProt Gene: CTADII UniProt Name: Cytochrome c oxidase polypeptide I-beta PIR Number: S08270	1QLE PDB Title: Cytochrome C Oxidase Polypeptide I-Beta	Iwata et al. (1995). Iwata S, Ostermeier C, Ludwig B, & Michel H (1995). Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 :660-669. PubMed Id: 7651515.
*cyto. C oxidase. Subunit II: Paracoccus denitrificans* B Bacteria** Chain B in PDB file. See also J.Biol.Chem. (1999) 274:33296-33299. Nterm in = cytoplasm. Sequence is processed sequence from Swiss-Prot (29 AA signal sequence removed). TMhelices=2. N Terminal: out TM Segment Count: 2 TM Segments: A.27,59; B.74,105; Sequence: QDVLGDLPVIGKPVNGGMNFQPASSPLAHDQQWLDHFVLYIITAVTIFVCLLLLICIVRFNRRANPVPARFTHNTPIEVIWTLVPVLILVAIGAFSLPILFRSQEMPNDPDLVIKAIGHQWYWSYEYPNDGVAFDALMLEKEALADAGYSEDEYLLATDNPVVVPVGKKVLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAKEEFAADASDYLPASPVKLASAE	P08306 UniProt Entry: COX2_PARDE UniProt Gene: CTAC, CTAB, COII UniProt Name: Cytochrome c oxidase polypeptide II [Precursor] PIR Number:	1QLE PDB Title: Cytochrome C Oxidase Polypeptide II	Iwata et al. (1995). Iwata S, Ostermeier C, Ludwig B, & Michel H (1995). Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 :660-669. PubMed Id: 7651515.
*cyto. C oxidase. Subunit III: Paracoccus denitrificans* B Bacteria** Chain C in PDB file. Nterm in = cytoplasm. See also J. Biol. Chem. (1999), 274:33296-33299. Sequence from Swiss Prot. TMhelices=7. N Terminal: in TM Segment Count: 7 TM Segments: A.15,35; B.48,76; C.79,114; D.139,165; E.168,196; F.203,236; G.244,273; Sequence: AHVKNHDYQILPPSIWPFFGAIGAFVMLTGAVAWMKGITFFGLPVEGPWMFLIGLVGVLYVMFGWWADVVNEGETGEHTPVVRIGLQYGFILFIMSEVMFFVAWFWAFIKNALYPMGPDSPIKDGVWPPEGIVTFDPWHLPLINTLILLLSGVAVTWAHHAFVLEGDRKTTINGLIVAVILGVCFTGLQAYEYSHAAFGLADTVYAGAFYMATGFHGAHVIIGTIFLFVCLIRLLKGQMTQKQHVGFEAAAWYWHFVDVVWLFLFVVIYIWGR	P06030 UniProt Entry: COX3_PARDE UniProt Gene: CTAE, COIII UniProt Name: Cytochrome c oxidase polypeptide III PIR Number: S03807	1QLE PDB Title: Cytochrome C Oxidase Polypeptide III	Iwata et al. (1995). Iwata S, Ostermeier C, Ludwig B, & Michel H (1995). Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 :660-669. PubMed Id: 7651515.
*cyto. C oxidase. Subunit IV: Paracoccus denitrificans* B Bacteria** Chain D in PDB file. See also J. Biol. Chem. (1999), 274:33296-33299. Sequence from Swiss Prot. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.17,48; Sequence: ASHHEITDHKHGEMDIRHQQATFAGFIKGATWVSILSIAVLVFLALANS	P77921 UniProt Entry: COX4_PARDE UniProt Gene: CTAH UniProt Name: Cytochrome c oxidase polypeptide IV PIR Number: S03807	1QLE PDB Title: Cytochrome C Oxidase	Iwata et al. (1995). Iwata S, Ostermeier C, Ludwig B, & Michel H (1995). Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 :660-669. PubMed Id: 7651515.
*cyto.c oxidase. Chain I: Thermus thermophilus* B Bacteria** Chain A in PDB file. Sequence from Swiss-Prot. cytoplasm = in. TMhelices=13. N Terminal: in TM Segment Count: 13 TM Segments: A.17,48; B.65,97; C.103,125; D.143,173; E.181,212; F.221,254; G.262,283; H.292,326; I.344,366; J.380,409; K.415,444; L.461,493; M.527,550; Sequence: MAVRASEISRVYEAYPEKKATLYFLVLGFLALIVGSLFGPFQALNYGNVDAYPLLKRLLPFVQSYYQGLTLHGVLNAIVFTQLFAQAIMVYLPARELNMRPNMGLMWLSWWMAFIGLVVAALPLLANEATVLYTFYPPLKGHWAFYLGASVFVLSTWVSIYIVLDLWRRWKAANPGKVTPLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADPGIDPTWKMIHSVLTLFVAVPSLMTAFTVAASLEFAGRLRGGRGLFGWIRALPWDNPAFVAPVLGLLGFIPGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAQRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAYIAQVPDAYPHAAVPMVFNVLAGIVLLVALLLFIYGLFSVLLSRERKPELAEAPLPFAEVISGPEDRRLVLAMDRIGFWFAVAAILVVLAYGPTLVQLFGHLNPVPGWRLW	Q56408 UniProt Entry: COX1_THETH UniProt Gene: CBAA UniProt Name: Cytochrome c oxidase polypeptide I PIR Number: T52481	1EHK PDB Title: Ba3-Type Cytochrome-C Oxidase, chain A	Soulimane et al. (2000). Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, & Than ME (2000). Structure and mechanism of the aberrant ba₃-cytochrome c oxidase from Thermus thermophilus. EMBO J 19 :1766-1776. PubMed Id: 10775261.
*cyto.c oxidase. Chain II: Thermus thermophilus* B Bacteria** Chain B in PDB file. Sequence from Swiss-Prot. cytoplasm = in. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.4,38; Sequence: MVDEHKAHKAILAYEKGWLAFSLAMLFVFIALIAYTLATHTAGVIPAGKLERVDPTTVRQEGPWADPAQAVVQTGPNQYTVYVLAFAFGYQPNPIEVPQGAEIVFKITSPDVIHGFHVEGTNINVEVLPGEVSTVRYTFKRPGEYRIICNQYCGLGHQNMFGTIVVKE	P98052 UniProt Entry: COX2_THETH UniProt Gene: CBAB, CTAC UniProt Name: Cytochrome c oxidase polypeptide II PIR Number: T52480	1EHK PDB Title: Ba3-Type Cytochrome-C Oxidase, chain B	Soulimane et al. (2000). Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, & Than ME (2000). Structure and mechanism of the aberrant ba₃-cytochrome c oxidase from Thermus thermophilus. EMBO J 19 :1766-1776. PubMed Id: 10775261.
*cyto.c oxidase. Chain IIa: Thermus thermophilus* B Bacteria** Chain C in PDB file. Sequence is from Swiss-Prot. cytoplasm = in. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.4,34; Sequence: MEEKPKGALAVILVLTLTILVFWLGVYAVFFARG	P82543 UniProt Entry: COXA_THETH UniProt Gene: CBAD UniProt Name: Cytochrome c oxidase polypeptide IIA PIR Number:	1EHK PDB Title: Ba3-Type Cytochrome-C Oxidase, chain C	Soulimane et al. (2000). Soulimane T, Than ME, Dewor M, Huber R, & Buse G (2000). Primary structure of a novel subunit in ba₃-cytochrome oxidase from Thermus thermophilus. Protein Sci 9 :2068-2073. PubMed Id: 11152118. doi:10.1110/ps.9.11.2068.
*ubiquinol oxidase subunit I: Escherichia coli* B Bacteria** Sequence is from Swiss-Prot. Helices A & O are not reported in the 1EFT structure file. Their assignments are from Swiss-Prot. N Terminal: out TM Segment Count: 15 TM Segments: A.17,35; B.53,80; C.96,132; D.138,161; E.185,215; F.225,260; G.271,307; H.312,326; I.341,369; J.378,409; K.413,445; L.449,477; M.490,521; N.588,606; O.614,632; Sequence: MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQFHTMLMIAASGAVLIALGILCLVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN	P18401 UniProt Entry: CYOB_ECOLI UniProt Gene: CYOB, B0431, C0542, Z0534, ECS0485 UniProt Name: Ubiquinol oxidase polypeptide I PIR Number: A85540, B42226, E90689	1FFT PDB Title: Ubiquinol Oxidase, Chain A	Abramson et al. (2000). Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, & Wikstrom M (2000). The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat Struct Biol 7 :910-917. PubMed Id: 11017202.
*ubiquinol oxidase subunit II: Escherichia coli* B Bacteria** Sequence is from Swiss-Prot. This corresponds to chain B in PDB file. Although the sequence has a signal sequence, helix numbering is for unprocessed sequence. N Terminal: out TM Segment Count: 2 TM Segments: A.37,70; B.87,113; Sequence: MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAAFDQWVAKAKQSPNTMSDMAAFEKLAAPSEYNQVEYFSNVKPDLFADVINKFMAHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH	P0ABJ1 UniProt Entry: CYOA_ECOLI UniProt Gene: cyoA UniProt Name: Ubiquinol oxidase polypeptide II [precursor] PIR Number: A42226	1FFT PDB Title: Ubiquinol Oxidase, Chain B	Abramson et al. (2000). Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, & Wikstrom M (2000). The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat Struct Biol 7 :910-917. PubMed Id: 11017202.
*ubiquinol oxidase subunit III: Escherichia coli* B Bacteria** Sequence from Swiss-Prot. N Terminal: in TM Segment Count: 5 TM Segments: A.21,48; B.64,91; C.95,125; D.139,166; E.175,200; Sequence: MATDTLTHATAHAHEHGHHDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM	P18402 UniProt Entry: CYOC_ECOLI UniProt Gene: CYOC, B0430, C0541, SF0371, S0376 UniProt Name: Cytochrome o ubiquinol oxidase subunit III PIR Number: C4226	1FFT PDB Title: Ubiquinol Oxidase, Chain C	Abramson et al. (2000). Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, & Wikstrom M (2000). The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat Struct Biol 7 :910-917. PubMed Id: 11017202.
Electron Transport Chain Supercomplexes (Respirasome)
Nitric Oxide Reductases
Photosystems
*photosystem I A subunit: Synechococcus elongatus* B Bacteria** Stroma=in. Sequence from Swiss-Prot. TMhelices=11. N Terminal: in TM Segment Count: 11 TM Segments: A.65,97; B.155,181; C.193,227; D.294,311; E.352,376; F.387,418; G.437,468; H.533,558; I.591,620; J.670,691; K.724,755; Sequence: MTISPPEREPKVRVVVDNDPVPTSFEKWAKPGHFDRTLARGPQTTTWIWNLHALAHDFDTHTSDLEDISRKIFSAHFGHLAVVFIWLSGMYFHGAKFSNYEAWLADPTGIKPSAQVVWPIVGQGILNGDVGGGFHGIQITSGLFQLWRASGITNEFQLYCTAIGGLVMAGLMLFAGWFHYHKRAPKLEWFQNVESMLNHHLAGLLGLGSLAWAGHQIHVSLPINKLLDAGVAAKDIPLPHEFILNPSLMAELYPKVDWGFFSGVIPFFTFNWAAYSDFLTFNGGLNPVTGGLWLSDTAHHHLAIAVLFIIAGHMYRTNWGIGHSLKEILEAHKGPFTGAGHKGLYEVLTTSWHAQLAINLAMMGSLSIIVAQHMYAMPPYPYLATDYPTQLSLFTHHMWIGGFLVVGGAAHGAIFMVRDYDPAMNQNNVLDRVLRHRDAIISHLNWVCIFLGFHSFGLYVHNDTMRAFGRPQDMFSDTGIQLQPVFAQWVQNLHTLAPGGTAPNAAATASVAFGGDVVAVGGKVAMMPIVLGTADFMVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSGWDHVFLGLFWMYNCISVVIFHFSWKMQSDVWGTVAPDGTVSHITGGNFAQSAITINGWLRDFLWAQASQVIGSYGSALSAYGLLFLGAHFIWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPAIQPRALSIIQGRAVGVAHYLLGGIATTWAFFLARIISVG	P25896 UniProt Entry: PSAA_SYNEL UniProt Gene: PSAA, TLR0731 UniProt Name: Photosystem I P700 chlorophyll A apoprotein A1 PIR Number:	1JB0 PDB Title: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1	Jordan et al. (2001). Jordan P, Fromme P, Witt HT, Klukas O, Saenger W, & Krauss N (2001). Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411 :909-917. PubMed Id: 11418848.
*photosystem I B subunit: Synechococcus elongatus* B Bacteria** Stroma=in. Sequence from Swiss-Prot. TMhelices=11. N Terminal: in TM Segment Count: 11 TM Segments: A.38,70; B.131,154; C.170,201; D.269,286; E.333,357; F.368,399; G.418,448; H.520,545; I.578,609; J.650,671; K.707,738; Sequence: ATKFPKFSQDLAQDPTTRRIWYAIAMAHDFESHDGMTEENLYQKIFASHFGHLAIIFLWVSGSLFHVAWQGNFEQWVQDPVNTRPIAHAIWDPQFGKAAVDAFTQAGASNPVDIAYSGVYHWWYTIGMRTNGDLYQGAIFLLILASLALFAGWLHLQPKFRPSLSWFKNAESRLNHHLAGLFGVSSLAWAGHLIHVAIPESRGQHVGWDNFLSTMPHPAGLAPFFTGNWGVYAQNPDTASHVFGTAQGAGTAILTFLGGFHPQTESLWLTDMAHHHLAIAVLFIVAGHMYRTQFGIGHSIKEMMDAKDFFGTKVEGPFNMPHQGIYETYNNSLHFQLGWHLACLGVITSLVAQHMYSLPPYAFIAQDHTTMAALYTHHQYIAGFLMVGAFAHGAIFLVRDYDPAQNKGNVLDRVLQHKEAIISHLSWVSLFLGFHTLGLYVHNDVVVAFGTPEKQILIEPVFAQFIQAAHGKLLYGFDTLLSNPDSIASTAWPNYGNVWLPGWLDAINSGTNSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYAFPCDGPGRGGTCDISAWDAFYLAMFWMLNTIGWVTFYWHWKHLGVWEGNVAQFNESSTYLMGWLRDYLWLNSSQLINGYNPFGTNNLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLVWAHERTPLANLVRWKDKPVALSIVQARLVGLAHFSVGYILTYAAFLIASTAAKFG	P25897 UniProt Entry: PSAB_SYNEL UniProt Gene: PSAB, TLR0732 UniProt Name: Photosystem I P700 chlorophyll A apoprotein A2 PIR Number:	1JB0 PDB Title: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2	Jordan et al. (2001). Jordan P, Fromme P, Witt HT, Klukas O, Saenger W, & Krauss N (2001). Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411 :909-917. PubMed Id: 11418848.
*photosystem I F subunit : Synechococcus elongatus B Bacteria** *Only helix A is transmembrane. Helix B does not cross the membrane, but is buried in it with a kink so that it enters and leaves from the same side (stromal) of the membrane. Stroma = in. Sequence is the processed sequence from Swiss-Prot (23 AA signal sequence removed). N Terminal: out TM Segment Count: 2 TM Segments: A.64,89; B.104,126; Sequence: DVAGLVPCKDSPAFQKRAAAAVNTTADPASGQKRFERYSQALCGEDGLPHLVVDGRLSRAGDFLIPSVLFLYIAGWIGWVGRAYLIAVRNSGEANEKEIIIDVPLAIKCMLTGFAWPLAALKELASGELTAKDNEITVSPR	P0A401 UniProt Entry: PSAF_SYNEL UniProt Gene: PSAF, TLR2411 UniProt Name: Photosystem I reaction centre subunit III [Precursor] PIR Number:	1JB0 PDB Title: PHOTOSYSTEM 1 REACTION CENTRE SUBUNIT III	Jordan et al. (2001). Jordan P, Fromme P, Witt HT, Klukas O, Saenger W, & Krauss N (2001). Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411 :909-917. PubMed Id: 11418848.
*photosystem I I subunit: Synechococcus elongatus* B Bacteria** Stroma=in. Sequence from Swiss-Prot. TMhelices=1. N Terminal: out TM Segment Count: 1 TM Segments: A.10,35; Sequence: MMGSYAASFLPWIFIPVVCWLMPTVVMGLLFLYIEGEA	P25900 UniProt Entry: PSAI_SYNEL UniProt Gene: PSAI, TSR2405 UniProt Name: Photosystem I reaction center subunit VIII PIR Number:	1JB0 PDB Title: PHOTOSYSTEM 1 REACTION CENTRE SUBUNIT VIII	Jordan et al. (2001). Jordan P, Fromme P, Witt HT, Klukas O, Saenger W, & Krauss N (2001). Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411 :909-917. PubMed Id: 11418848.
*photosystem I J subunit: Synechococcus elongatus* B Bacteria** Stroma=in. Sequence from Swiss-Prot. TMhelices=1. N Terminal: out TM Segment Count: 1 TM Segments: A.11,31; Sequence: MKHFLTYLSTAPVLAAIWMTITAGILIEFNRFYPDLLFHPL	P25901 UniProt Entry: PSAJ_SYNEL UniProt Gene: PSAJ, TSR2412 UniProt Name: Photosystem I reaction center subunit IX PIR Number:	1JB0 PDB Title: PHOTOSYSTEM 1 REACTION CENTRE SUBUNIT IX	Jordan et al. (2001). Jordan P, Fromme P, Witt HT, Klukas O, Saenger W, & Krauss N (2001). Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411 :909-917. PubMed Id: 11418848.
*photosystem I K subunit: Synechococcus elongatus* B Bacteria** Stroma=in. Sequence is unprocessed sequence from Swiss-Prot, which corresponds to AA numbering in PDB file. TMhelices=2. N Terminal: out TM Segment Count: 2 TM Segments: A.20,36; B.55,77; Sequence: MVLATLPDTTWTPSVGLVVILCNLFAIALGRYAIQSRGKGPGLPIALPALFEGFGLPELLATTSFGHLLAAGVVSGLQYAGAL	P20453 UniProt Entry: PSAK_SYNEL UniProt Gene: PSAK, TSR2273 UniProt Name: Photosystem I reaction center subunit psaK [Precursor] PIR Number:	1JB0 PDB Title: PHOTOSYSTEM 1 REACTION CENTRE SUBUNIT X	Jordan et al. (2001). Jordan P, Fromme P, Witt HT, Klukas O, Saenger W, & Krauss N (2001). Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411 :909-917. PubMed Id: 11418848.
*photosystem I L subunit: Synechococcus elongatus* B Bacteria** Stroma = in. Sequence is from Swiss-Prot, with Met1 removed in order to agree with AA numbering in PDB file. TMhelices=3. N Terminal: in TM Segment Count: 3 TM Segments: A.43,65; B.74,99; C.114,140; Sequence: AEELVKPYNGDPFVGHLSTPISDSGLVKTFIGNLPAYRQGLSPILRGLEVGMAHGYFLIGPWVKLGPLRDSDVANLGGLISGIALILVATACLAAYGLVSFQKGGSSSDPLKTSEGWSQFTAGFFVGAMGSAFVAFFLLENFLVVDGIMTGLFN	P25902 UniProt Entry: PSAL_SYNEN UniProt Gene: PSAL, TLR2404 UniProt Name: Photosystem I subunit XI PIR Number:	1JB0 PDB Title: PHOTOSYSTEM 1 REACTION CENTRE SUBUNIT XI	Jordan et al. (2001). Jordan P, Fromme P, Witt HT, Klukas O, Saenger W, & Krauss N (2001). Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411 :909-917. PubMed Id: 11418848.
*photosystem I M subunit: Synechococcus elongatus* B Bacteria** Stroma=in. Sequence from Swiss-Prot. TMhelices=1. N Terminal: out TM Segment Count: 1 TM Segments: A.6,30; Sequence: MALTDTQVYVALVIALLPAVLAFRLSTELYK	P25903 UniProt Entry: PSAM_SYNEL UniProt Gene: PSAM, TSR0197 UniProt Name: Photosystem I reaction centre subunit XII PIR Number:	1JB0 PDB Title: PHOTOSYSTEM 1 REACTION CENTRE SUBUNIT XII	Jordan et al. (2001). Jordan P, Fromme P, Witt HT, Klukas O, Saenger W, & Krauss N (2001). Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411 :909-917. PubMed Id: 11418848.
*photosystem I X subunit: Synechococcus elongatus* B Bacteria** Stroma=in. Sequence from TrEMBL. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.11,31; Sequence: ATKSAKPTYAFRTFWAVLLLAINFLVAAYYFAAAA	Q8DKP6 UniProt Entry: Q8DKP6 UniProt Gene: TSR0813 UniProt Name: Photosystem I 4.8K protein PIR Number:	1JB0 PDB Title: X PHOTOSYSTEM I SUBUNIT PSAX	Jordan et al. (2001). Jordan P, Fromme P, Witt HT, Klukas O, Saenger W, & Krauss N (2001). Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411 :909-917. PubMed Id: 11418848.
*Photosystem II Q(B) protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain A in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: in TM Segment Count: 5 TM Segments: A.34,54; B.111,136; C.145,158; D.199,221; E.268,295; Sequence: MTTTLQRRESANLWERFCNWVTSTDNRLYVGWFGVIMIPTLLAATICFVIAFIAAPPVDIDGIREPVSGSLLYGNNIITGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLIIFHFLLGASCYMGRQWELSYRLGMRPWICVAYSAPLASAFAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHQLGVAGVFGGALFCAMHGSLVTSSLIRETTETESANYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGVWFTALGISTMAFNLNGFNFNHSVIDAKGNVINTWADIINRANLGMEVMHERNAHNFPLDLASAESAPVAMIAPSING	P0A444 UniProt Entry: PSBA1_SYNEL UniProt Gene: psbA1 UniProt Name: Photosystem Q(B) protein PIR Number: S26586	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*photosystem II core light harvesting protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain B in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: in TM Segment Count: 6 TM Segments: A.16,44; B.93,112; C.135,155; D.196,214; E.236,258; F.447,472; Sequence: MGLPWYRVHTVLINDPGRLIAAHLMHTALVAGWAGSMALYELATFDPSDPVLNPMWRQGMFVLPFMARLGVTGSWSGWSITGETGIDPGFWSFEGVALAHIVLSGLLFLAACWHWVYWDLELFRDPRTGEPALDLPKMFGIHLFLAGLLCFGFGAFHLTGLFGPGMWVSDPYGLTGSVQPVAPEWGPDGFNPYNPGGVVAHHIAAGIVGIIAGLFHILVRPPQRLYKALRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDSSYFQQEINRRVQASLASGATLEEAWSAIPEKLAFYDYIGNNPAKGGLFRTGPMNKGDGIAQAWKGHAVFRNKEGEELFVRRMPAFFESFPVILTDKNGVVKADIPFRRAESKYSFEQQGVTVSFYGGELNGQTFTDPPTVKSYARKAIFGEIFEFDTETLNSDGIFRTSPRGWFTFAHAVFALLFFFGHIWHGARTLFRDVFSGIDPELSPEQVEWGFYQKVGDVTTRRKEAV	Q8DIQ1 UniProt Entry: Q8DIQ1_SYNEL UniProt Gene: psbB UniProt Name: Photosystem II core light harvesting protein PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II CP43 protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain C in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: in TM Segment Count: 6 TM Segments: A.49,74; B.111,134; C.154,177; D.231,253; E.268,291; F.423,446; Sequence: MKTLSSQKRYSPVVTLSSNSIFATNRDQESSGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMTLFELAHFIPEKPMYEQGLILIPHIATLGWGVGPGGEVVDTFPFFVVGVVHLISSAVLGFGGVYHAIRGPETLEEYSSFFGYDWKDKNKMTTILGFHLIVLGIGALLLVAKAMFFGGLYDTWAPGGGDVRVITNPTLDPRVIFGYLLKSPFGGEGWIVSVNNLEDVVGGHIWIGLICIAGGIWHILTTPFGWARRAFIWSGEAYLSYSLGALSMMGFIATCFVWFNNTVYPSEFYGPTGPEASQAQAMTFLIRDQKLGANVGSAQGPTGLGKYLMRSPTGEIIFGGETMRFWDFRGPWLEPLRGPNGLDLNKIKNDIQPWQERRAAEYMTHAPLGSLNSVGGVATEINSVNFVSPRSWLATSHFVLAFFFLVGHLWHAGRARAAAAGFEKGIDRESEPVLSMPSLD	Q8DIF8 UniProt Entry: Q8DIF8_SYNEL UniProt Gene: psbC UniProt Name: Photosystem II CP43 protein PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II D2 protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain D in PDB file. TM C and E contains of two helices. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: in TM Segment Count: 5 TM Segments: A.34,54; B.110,131; C.142,157; D.195,220; E.265,289; Sequence: MTIAIGRAPAERGWFDILDDWLKRDRFVFVGWSGILLFPCAYLALGGWLTGTTFVTSWYTHGLASSYLEGCNFLTVAVSTPANSMGHSLLLLWGPEAQGDFTRWCQLGGLWTFIALHGAFGLIGFMLRQFEIARLVGVRPYNAIAFSAPIAVFVSVFLIYPLGQSSWFFAPSFGVAAIFRFLLFFQGFHNWTLNPFHMMGVAGVLGGALLCAIHGATVENTLFQDGEGASTFRAFNPTQAEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWMSAIGVVGLALNLRSYDFISQEIRAAEDPEFETFYTKNLLLNEGIRAWMAPQDQPHENFVFPEEVLPRGNAL	Q8CM25 UniProt Entry: Q8CM25_SYNEL UniProt Gene: psbD2 UniProt Name: Photosystem II reaction center D2 protein PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II Cytochrome b559 alpha subunit: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain E in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: in TM Segment Count: 1 TM Segments: A.16,38; Sequence: AGTTGERPFSDIITSVRYWVIHSITIPALFIAGWLFVSTGLAYDVFGTPRPDSYYAQEQRSIPLVTDRFEAKQQVETFLEQLK	Q8DIP0 UniProt Entry: PSBE_SYNEL UniProt Gene: psbE UniProt Name: Cytochrome b559 alpha subunit PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II Cytochrome b559 beta subunit: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain F in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: in TM Segment Count: 1 TM Segments: A.16,39; Sequence: MTSNTPNQEPVSYPIFTVRWVAVHTLAVPTIFFLGAIAAMQFIQR	Q8DIN9 UniProt Entry: PSBF_SYNEL UniProt Gene: psbF UniProt Name: Cytochrome b559 subunit beta PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II PsbH protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain H in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: in TM Segment Count: 1 TM Segments: A.27,48; Sequence: MARRTWLGDILRPLNSEYGKVAPGWGTTPLMAVFMGLFLVFLLIILEIYNSTLILDGVNVSWKALG	Q8DJ43 UniProt Entry: PSBH_SYNEL UniProt Gene: psbH UniProt Name: photosystem II reaction center protein H PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II PsbI protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain I in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: out TM Segment Count: 1 TM Segments: A.3,20; Sequence: METLKITVYIVVTFFVLLFVFGFLSGDPARNPKRKDLE	Q8DJZ6 UniProt Entry: PSBI_SYNEL UniProt Gene: psbI UniProt Name: Photosystem II reaction center protein I PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II PsbJ protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain J in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: in TM Segment Count: 1 TM Segments: A.13,30; Sequence: MMSEGGRIPLWIVATVAGMGVIVIVGLFFYGAYAGLGSSL	P59087 UniProt Entry: PSBJ_SYNEL UniProt Gene: psbJ UniProt Name: Photosystem II reaction center protein J PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II PsbK protein: Thermosynechococcus elongatus* B Bacteria** Sequence from PDB, chain K. In Swiss-Prot file there is aditional 9 aa at the beginning so res#1 in PBD file corresponds to res#10 in Swiss-Prot file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: out TM Segment Count: 1 TM Segments: A.4,33; Sequence: KLPEAYAIFDPLVDVLPVIPVLFLALAFVWQAAVGFR	Q9F1K9 UniProt Entry: PSBK_SYNEL UniProt Gene: psbK UniProt Name: Photosystem II reaction center protein K PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II PsbL protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain L in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: in TM Segment Count: 1 TM Segments: A.14,36; Sequence: MEPNPNRQPVELNRTSLYLGLLLILVLALLFSSYFFN	Q8DIN8 UniProt Entry: PSBL_SYNEL UniProt Gene: psbL UniProt Name: Photosystem II reaction center protein L PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II PsbM protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain M in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: out TM Segment Count: 1 TM Segments: A.6,29; Sequence: MEVNQLGLIATALFVLVPSVFLIILYVQTESQQKSS	Q8DHA7 UniProt Entry: PSBM_SYNEL UniProt Gene: psbM UniProt Name: Photosystem II reaction center protein M PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II PsbT protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain T in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: out TM Segment Count: 1 TM Segments: A.5,22; Sequence: METITYVFIFACIIALFFFAIFFREPPRITKK	Q8DIQ0 UniProt Entry: PSBT_SYNEL UniProt Gene: psbT UniProt Name: photosystem II reaction center protein T PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II PsbX protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain X in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: out TM Segment Count: 1 TM Segments: A.15,43; Sequence: MIQSASSLLLTITPSLKGFFIGLLSGAVVLGLTFAVLIAISQIDKVQRSL	Q8DHE6 UniProt Entry: Q8DHE6_SYNEL UniProt Gene: psbX UniProt Name: photosystem II PsbX protein PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II PsbN protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain N in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: out TM Segment Count: 1 TM Segments: A.2,30; Sequence: MEPATVLSIALAAVCIGVTGYSIYLSFGPPSKELADPFDDHED	Q8DJ42 UniProt Entry: PSBN_SYNEL UniProt Gene: psbN UniProt Name: Photosystem II reaction center protein N PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II PsbZ protein: Thermosynechococcus elongatus* B Bacteria** Sequence from Swiss-Prot. This corresponds to chain Z in PDB file. See also 1FE1(earlier lower resolution structure)and 2AXT(later higher resolution structure). Stroma=in. N Terminal: out TM Segment Count: 2 TM Segments: A.2,19; B.33,56; Sequence: MTILFQLALAALVILSFVMVIGVPVAYASPQDWDRSKQLIFLGSGLWIALVLVVGVLNFFVV	Q8DHJ2 UniProt Entry: PSBZ_SYNEL UniProt Gene: psbZ UniProt Name: Photosystem II reaction center protein Z PIR Number:	1S5L PDB Title: Architecture of the photosynthetic oxygen evolving center	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
Light-Harvesting Complexes
*Light Harvesting Complex. alpha chain: Rhodopseudomonas acidophila* B Bacteria** Chain A of PDB file. Sequence from Swiss-Prot. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.11,36; Sequence: MNQGKIWTVVNPAIGIPALLGSVTVIAILVHLAILSHTTWFPAYWQGGVKKAA	P26789 UniProt Entry: LHA4_RHOAC UniProt Gene: UniProt Name: Light-harvesting protein B-800/850, alpha chain PIR Number: S06365	1KZU PDB Title: integral membrane peripheral light harvesting complex from Rhodopseudomonas acidophila strain 10050	McDermott et al. (1995) McDermott G, Prince SM, Freer AA, Hawthornthwaite-Lawless AM, Papiz MZ, Cogdell RJ & Isaacs NW (1995). Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria. Nature 374 :517-521. doi:10.1038/374517a0.
*Light Harvesting Complex. beta chain: Rhodopseudomonas acidophila* B Bacteria** Chain B of PDB file. Sequence from Swiss-Prot. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.11,36; Sequence: ATLTAEQSEELHKYVIDGTRVFLGLALVAHFLAFSATPWLH	P26790 UniProt Entry: LHB5_RHOAC UniProt Gene: UniProt Name: Light-harvesting protein B-800/850, beta chain PIR Number: S07673	1KZU PDB Title: integral membrane peripheral light harvesting complex from Rhodopseudomonas acidophila strain 10050	McDermott et al. (1995) McDermott G, Prince SM, Freer AA, Hawthornthwaite-Lawless AM, Papiz MZ, Cogdell RJ & Isaacs NW (1995). Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria. Nature 374 :517-521. doi:10.1038/374517a0.
*Light Harvesting Complex. alpha chain: Rhodospirillum molischianum* B Bacteria** Chain A of PDB file. Sequence from Swiss-Prot. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.16,40; Sequence: SNPKDDYKIWLVINPSTWLPVIWIVATVVAIAVHAAVLAAPGSNWIALGAAKSAAK	P97253 UniProt Entry: LHA_RHOMO UniProt Gene: A1, A2, A3 UniProt Name: Light-harvesting protein B-800/850, alpha chain PIR Number: A49290	1LGH PDB Title: crystal structure of the light-harvesting complex II 2 (B00-850) from Rhodospirillum molischianum	Koepke et al. (1996). Koepke J, Hu XC, Muenke C, Schulten K, & Michel H (1996). The crystal structure of the light-harvesting complex II (B800- 850) from Rhodospirillum molischianum. Structure 4 :581-597. PubMed Id: 8736556.
*Light Harvesting Complex. beta chain: Rhodospirillum molischianum* B Bacteria** Chain B in PDB file. Sequence from Swiss-Prot. TMhelices=1. N Terminal: in TM Segment Count: 1 TM Segments: A.10,41; Sequence: AERSLSGLTEEEAIAVHDQFKTTFSAFIILAAVAHVLVWVWKPWF	P95673 UniProt Entry: LHB1_RHOMO UniProt Gene: B1 UniProt Name: Light-harvesting protein B-800/850, beta 1 chain PIR Number: B49290	1LGH PDB Title: crystal structure of the light-harvesting complex II 2 (B00-850) from Rhodospirillum molischianum	Koepke et al. (1996). Koepke J, Hu XC, Muenke C, Schulten K, & Michel H (1996). The crystal structure of the light-harvesting complex II (B800- 850) from Rhodospirillum molischianum. Structure 4 :581-597. PubMed Id: 8736556.
*LHC-II: Spinacia oleracea* E Eukaryota** Sequence is from Swiss-Prot. The 35AA pre-sequence has been removed, consistent with PDB sequence. Stroma=in. N Terminal: in TM Segment Count: 3 TM Segments: A.55,86; B.124,144; C.170,201; Sequence: RKTAGKPKTVQSSSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFAKNRELEVIHCRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSEGGLDYLGNPSLVHAQSILAIWACQVILMGAVEGYRIAGGPLGEVVDPLYPGGSFDPLGLADDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVNNNAWNFATNFVPGK	P12333 UniProt Entry: CB21_SPIOL UniProt Gene: UniProt Name: Chlorophyll a-b binding protein, chloroplast [Precursor] PIR Number: JQ0020	1RWT PDB Title: Chlorophyll A-B Binding Protein, Chloroplast	Liu et al. (2004). Liu Z, Yan H, Wang K, Kuang T, Zhang J, Gui L, An X, & Chang W (2004). Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution. Nature 428 :287-292. PubMed Id: 15029188.
Photosystem+Light-Harvesting Complex Supercomplex
Photoprotection Proteins These proteins limit photo-oxidative damage to plants
Photosynthetic Reaction Centers
*Reaction center. Chain H: Rhodopseudomonas* B Bacteria** Sequence from Swiss-Prot. TMhelices=1. N Terminal: out TM Segment Count: 1 TM Segments: A.12,37; Sequence: MYHGALAQHLDIAQLVWYAQWLVIWTVVLLYLRREDRREGYPLVEPLGLVKLAPEDGQVYELPYPKTFVLPHGGTVTVPRRRPETRELKLAQTDGFEGAPLQPTGNPLVDAVGPASYAERAEVVDATVDGKAKIVPLRVATDFSIAEGDVDPRGLPVVAADGVEAGTVTDLWVDRSEHYFRYLELSVAGSARTALIPLGFCDVKKDKIVVTSILSEQFANVPRLQSRDQITLREEDKVSAYYAGGLLYATPERAESLL	P06008 UniProt Entry: RCEH_RHOVI UniProt Gene: PUHA UniProt Name: Reaction center protein H chain PIR Number: A22841	1PRC PDB Title: photosynthetic reaction center	Deisenhofer et al. (1985). Deisenhofer J, Epp O, Miki K, Huber R, & Michel H (1985). Structure of the protein subunits in the photosynthetic reaction centre of Rhodospeudomonas viridis at 3 Å resolution. Nature 318 :618-624. PubMed Id: 22439175.
*Reaction center. Chain L: Rhodopseudomonas* B Bacteria** Sequence from Swiss-Prot. TMhelices=5. N Terminal: in TM Segment Count: 5 TM Segments: A.32,55; B.84,112; C.115,140; D.170,199; E.225,251; Sequence: ALLSFERKYRVRGGTLIGGDLFDFWVGPYFVGFFGVSAIFFIFLGVSLIGYAASQGPTWDPFAISINPPDLKYGLGAAPLLEGGFWQAITVCALGAFISWMLREVEISRKLGIGWHVPLAFCVPIFMFCVLQVFRPLLLGSWGHAFPYGILSHLDWVNNFGYQYLNWHYNPGHMSSVSFLFVNAMALGLHGGLILSVANPGDGDKVKTAEHENQYFRDVVGYSIGALSIHRLGLFLASNIFLTGAFGTIASGPFWTRGWPEWWGWWLDIPFWS	P06009 UniProt Entry: RCEL_RHOVI UniProt Gene: PUFL UniProt Name: Reaction center protein L chain PIR Number: A25102	1PRC PDB Title: photosynthetic reaction center	Deisenhofer et al. (1985). Deisenhofer J, Epp O, Miki K, Huber R, & Michel H (1985). Structure of the protein subunits in the photosynthetic reaction centre of Rhodospeudomonas viridis at 3 Å resolution. Nature 318 :618-624. PubMed Id: 22439175.
*Reaction center. Chain M: Rhodopseudomonas* B Bacteria** Sequence from Swiss-Prot. TMhelices=5. N Terminal: in TM Segment Count: 5 TM Segments: A.52,78; B.110,139; C.142,167; D.197,225; E.259,285; Sequence: ADYQTIYTQIQARGPHITVSGEWGDNDRVGKPFYSYWLGKIGDAQIGPIYLGASGIAAFAFGSTAILIILFNMAAEVHFDPLQFFRQFFWLGLYPPKAQYGMGIPPLHDGGWWLMAGLFMTLSLGSWWIRVYSRARALGLGTHIAWNFAAAIFFVLCIGCIHPTLVGSWSEGVPFGIWPHIDWLTAFSIRYGNFYYCPWHGFSIGFAYGCGLLFAAHGATILAVARFGGDREIEQITDRGTAVERAALFWRWTIGFNATIESVHRWGWFFSLMVMVSASVGILLTGTFVDNWYLWCVKHGAAPDYPAYLPATPDPASLPGAPK	P06010 UniProt Entry: RCEM_RHOVI UniProt Gene: PUFM UniProt Name: Reaction center protein M chain PIR Number: B25102	1PRC PDB Title: photosynthetic reaction center	Deisenhofer et al. (1985). Deisenhofer J, Epp O, Miki K, Huber R, & Michel H (1985). Structure of the protein subunits in the photosynthetic reaction centre of Rhodospeudomonas viridis at 3 Å resolution. Nature 318 :618-624. PubMed Id: 22439175.
*Reaction center. Chain H: Rhodobacter sphaeroides* B Bacteria** Sequence from Swiss-Prot. TMhelices=1. N Terminal: out TM Segment Count: 1 TM Segments: A.13,36; Sequence: MVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPKPKTFILPHGRGTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHNKIKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQMARFLEVELKDGSTRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVAGGLMYAAPKRKSVVAAMLAEYA	P11846 UniProt Entry: RCEH_RHOSH UniProt Gene: PUHA UniProt Name: Reaction center protein H chain PIR Number: A26538	2RCR 4RCR PDB Title: Photosynthetic reaction center from (Rhodobacter sphaeroides)	Allen et al. (1987). Allen JP, Feher G, Yeates TO, Komiya H, & Rees DC (1987). Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. Proc Natl Acad Sci USA 84 :6162-6166. PubMed Id: 2819866.
*Reaction center. Chain L: Rhodobacter sphaeroides* B Bacteria** Sequence from Swiss-Prot. TMhelices=5. N Terminal: in TM Segment Count: 5 TM Segments: A.32,55; B.84,111; C.115,140; D.170,199; E.225,251; Sequence: ALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWNPQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFAFAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAISFFFTNALALALHGALVLSAANPEKGKEMRTPDHEDTFFRDLVGYSIGTLGIHRLGLLLSLSAVFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING	P02954 UniProt Entry: RCEL_RHOSH UniProt Gene: PUFL UniProt Name: Reaction center protein L chain PIR Number: WNRFLS	2RCR 4RCR PDB Title: Photosynthetic reaction center from (Rhodobacter sphaeroides)	Allen et al. (1987). Allen JP, Feher G, Yeates TO, Komiya H, & Rees DC (1987). Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. Proc Natl Acad Sci USA 84 :6162-6166. PubMed Id: 2819866.
*Reaction center. Chain M: Rhodobacter sphaeroides* B Bacteria** Sequence from Swiss-Prot. TMhelices=5. N Terminal: in TM Segment Count: 5 TM Segments: A.52,77; B.110,139; C.142,167; D.197,224; E.259,285; Sequence: AEYQNIFSQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLSLFSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIASFFMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGIFSHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSALLFAMHGATILAVSRFGGERELEQIADRGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQNHGMAPLN	P02953 UniProt Entry: RCEM_RHOSH UniProt Gene: PUFM UniProt Name: Reaction center protein M chain PIR Number: WNRFMS	2RCR 4RCR PDB Title: Photosynthetic reaction center from (Rhodobacter sphaeroides)	Allen et al. (1987). Allen JP, Feher G, Yeates TO, Komiya H, & Rees DC (1987). Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. Proc Natl Acad Sci USA 84 :6162-6166. PubMed Id: 2819866.
*reaction center chain H: Thermochromatium tepidum* B Bacteria** Sequence from PDB. TMhelices=1. N Terminal: out TM Segment Count: 1 TM Segments: A.11,33; Sequence: MPAGITHYIDAAQITIWAFWLFFFGLIIYLRREDKREGYPLDSNRTERSGGRYKVVGFPDLPDPKTFVLPHNGGTVVAPRVEAPVAVNATPFSPAPGSPLVPNGDPMLSGFGPAASPDRPKHCDLTFEGLPKIVPMRVAKEFSIAEGDPDPRGMTVVGLDGEVAGTVSDVWVDRSEPQIRYLEVEVAANKKKVLLPIGFSRFDKKARKVKVDAIKAAHFANVPTLSNPDQVTLYEEDKVCAYYAGGKLYATAERAGPLL		1EYS PDB Title: Photosynthetic reaction center, H subunit	Nogi et al. (2000). Nogi T, Fathir I, Kobayashi M, Nozawa T, & Miki K (2000). Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer. Proc Natl Acad Sci USA 97 :6031-6036. PubMed Id: 11095707.
*reaction center chain L: Thermochromatium tepidum* B Bacteria** Sequence from PDB. TMhelices=5 N Terminal: in TM Segment Count: 5 TM Segments: A.33,55; B.93,119; C.124,147; D.179,205; E.234,258; Sequence: AMLSFEKKYRVRGGTLIGGDLFDFWVGPFYVGFFGVVGFCFTLLGVLLIVWGATIGPTGPTSDLQTYNLWRISIAPPDLSYGLRMAPLTEGGLWQIITICAAGAFISWALREVEICRKLGIGFHVPFAFSFAIGAYLVLVFVRPLLMGAWGHGFPYGILSHLDWVSNVGYQFLHFHYNPAHMLAISFFFTNCLALSMHGSLILSVTNPQRGEPVKTSEHENTFFRDIVGYSIGALAIHRLGLFLALSAAFWSAVCILISGPFWTRGWPEWWNWWLELPLW		1EYS PDB Title: Photosynthetic reaction center, L subunit	Nogi et al. (2000). Nogi T, Fathir I, Kobayashi M, Nozawa T, & Miki K (2000). Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer. Proc Natl Acad Sci USA 97 :6031-6036. PubMed Id: 11095707.
*reaction center chain M: Thermochromatium tepidum* B Bacteria** Sequence from PDB. TMhelices=5. N Terminal: in TM Segment Count: 5 TM Segments: A.54,77; B.112,134; C.144,167; D.196,224; E.265,284; Sequence: PEYQNIFTAVQVRAPAYPGVPLPKGNLPRIGRPIFSYWLGKIGDAQIGPIYLGLTGTLSIFFGLVAISIIGFNMLASVHWDVFQFLKHFFWLGLEPPPPQYGLRIPPLSEGGWWLIAGLFLTLSILLWWVRTYKRAEALGMSQHLSWAFAAAIFFYLVLGFIRPVMMGSWAKAVPFGIFPHLDWTAAFSIRYGNLYYNPFHMLSIAFLYGSALLFAMHGATILSVSRFGGDREIDQITHRGTAAEGAALFWRWTMGFNATMESIHRWAWWCAVLTVITAGIGILLSGTVVDNWYLWAVKHGMAPAYPEVVTAVNPYETAAEVMQ		1EYS PDB Title: Photosynthetic reaction center, M subunit	Nogi et al. (2000). Nogi T, Fathir I, Kobayashi M, Nozawa T, & Miki K (2000). Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer. Proc Natl Acad Sci USA 97 :6031-6036. PubMed Id: 11095707.
Light-Harvesting+Reaction Center Complexes

Description of Table

The table above is initially presented in a collapsed form, and the user can expand different sections of the table, or the entire table, and bookmark different sections of the table, or a fully expanded table version of the page, using the , , , and icons on the left margin of the table section headers.

Monotopic proteins and proteins with complex topologies, such as chloride channels, whose TM segments are not easily classified, are marked in the table by an asterisk ("*") following the protein name.

mpstruc and mptopo Taxonomic Domain data are derived from the UniProt Knowledgebase, which is based on the NCBI taxonomy database. These taxa can be searched for using 'Text Search of Table', above. The following icons are used in the table, as appropriate:

A : Archaea
B : Bacteria
E : Eukaryota
Vd : Viroids
V : Viruses
O : Other
U : Unclassified

from the Stephen White laboratory at UC Irvine

NOTES:

Description of Table