eF-site ID 6fkh-ABCDEFGHIJKLMNOPQRSTabdegp PDB Code 6fkh Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, a, b, d, e, g, p Title Chloroplast F1Fo conformation 2 Classification MEMBRANE PROTEIN Compound ATP synthase subunit a, chloroplastic Source ORGANISM_COMMON: Spinach; ORGANISM_SCIENTIFIC: Spinacia oleracea; Sequence A:  TIRADEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARI HGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEI TASESRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGR GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQK ASSVAQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYT GAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPP GREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVET QAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGI SVSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASD LDKATQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGT NGYLDSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTF TEEAEALLKEAIQEQMERFLLQ B:  KKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAG QPMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGA PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA PAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV GKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEM KESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTM AEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAV GYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ PRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEE DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIR GFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMESKL C:  IRADEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIH GLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMI QEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIT ASESRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGRG QRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKA SSVAQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTG AALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPG REAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQ AGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGIS VSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDL DKATQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTN GYLDSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTFT EEAEALLKEAIQEQMERFLLQ D:  KNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAGQ PMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGAP LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAP AFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG KTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMK ESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMA EYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVG YQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDP APATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP RIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEED RLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRG FQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMESKL E:  DEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIHGLD EVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEG SSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEITASE SRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGRGQRE LIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSV AQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTGAAL AEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREA YPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQAGD VSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR VGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDLDKA TQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTNGYL DSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTFTEEA EALLKEAIQEQMERFLL F:  KKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAG QPMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGA PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA PAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV GKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEM KESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTM AEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAV GYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ PRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEE DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIR GFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMES G:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV H:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV I:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV J:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV K:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV L:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV M:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV N:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV O:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV P:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV Q:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV R:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV S:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV T:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV a:  VGQHFYWQIGGFQIHGQVLITSWVVIAILLGSAAIAVRSP QTIPTGGQNFFEYVLEFIRDVSKTQIGEEYRPWVPFIGTM FLFIFVSNWSGALLPWKIIQLPHGELAAPTNDINTTVALA LLTSVAYFYAGLTKKGLGYFGKYIQPTPILLPINILEDFT KPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGL FTSGIQALIFATLAAAYIGESLE b:  FNTDILATNLINLSVVLGVLIFFGKGVLSDLLDNRKQRIL NTIRNSEELRGKAIEQLEKARARLKKVEMDADQFRVNGYS EIEREKMNLINSTYKTLEQFENYKNETIQFEQQKAINQVR QRVFQQALQGALGTLNSCLNNELHLRTINANIGMFGAMNE I d:  VDSTASRYASALADVADVTGTLEATNSDVEKLIRIFSEEP VYYFFANPVISIDNKRSVLDEIITTSGLQPHTANFINILI DSERINLVKEILNEFEDVFNKITGTEVAVVTSVVKLENDH LAQIAKGVQKITGAKNVRIKTVIDPSLVAGFTIRYGNEGS KLVDMSVKKQLEEIAAQLE e:  MTLNLCVLTPNRSIWNSEVKEIILSTNSGQIGVLPNHAPT ATAVDIGILRIRLNDQWLTLALMGGFARIGNNEITILVND AERGSDIDPQEAQQTLEIAEANLRKAEGKRQKIEANLALR RARTRVEASNT g:  NLRELRDRIGSVKNTQKITEAMKLVAAAKVRRAQEAVVNG RPFSETLVEVLYNMNEQLQTEDVDVPLTKIRTVKKVALMV VTGDRGLCGGFNNMLLKKAESRIAELKKLGVDYTIISIGK KGNTYFIRRPEIPVDRYFDGTNLPTAKEAQAIADDVFSLF VSEEVDKVEMLYTKFVSLVKSDPVIHTLLPLSPKGEICDI NGKCVDAAEDELFRLTTKEGKLTVERDMIKTETPAFSPIL EFEQDPAQILDALLPLYLNSQILRALQESLASELAARMTA MSNATDNANELKKTLSINYNRARQAKITGEILEIVAGANA C p:  IEKASLFDFNLTLPIIMAEFLFLMFALDKIYYTPLGDFMD KRDASIKEQLSGVKDTSSEVKQLEEQANAVMRAARAEISA ALNKMKKETQLEVEAKLAEGRKKIEVELQEALGSLEQQKE DTIKSLDSQISALSDDIVKKVLP Description (1)  ATP synthase subunit a, chloroplastic, ATP synthase subunit alpha, chloroplastic (E.C.3.6.3.14), ATP synthase subunit beta, chloroplastic (E.C.3.6.3.14), ATP synthase epsilon chain, chloroplastic, ATP synthase gamma chain, chloroplastic, ATP synthase subunit c, chloroplastic, ATP synthase subunit b', chloroplastic, ATP synthase subunit b, chloroplastic, ATP synthase delta chain, chloroplastic Functional site 1) chain D residue 363-372 type prosite sequence PAVDPLDSTS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS source prosite : PS00152 2) chain C residue 356-365 type prosite sequence PAINVGISVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS source prosite : PS00152 3) chain g residue 349-362 type prosite sequence ITGEILEIVAGANA description ATPASE_GAMMA ATP synthase gamma subunit signature. ITgEilEivaGAnA source prosite : PS00153 4) chain d residue 207-226 type prosite sequence VRIKTVIDPSLVAGFTIRYG description ATPASE_DELTA ATP synthase delta (OSCP) subunit signature. VrIktvIDpSLvAGFTIRyG source prosite : PS00389 5) chain a residue 185-194 type prosite sequence SLSFRLFGNI description ATPASE_A ATP synthase a subunit signature. SLSFRLFGNI source prosite : PS00449 6) chain S residue 40-61 type prosite sequence ARQPEAEGKIRGTLLLSLAFME description ATPASE_C ATP synthase c subunit signature. ARQPeaegkIrGtlLLslaFmE source prosite : PS00605 7) chain b residue 27-49 type TRANSMEM sequence LATNLINLSVVLGVLIFFGKGVL description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 8) chain Q residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 9) chain R residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 10) chain R residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 11) chain M residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 12) chain M residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 13) chain T residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 14) chain T residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 15) chain G residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 16) chain G residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 17) chain H residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 18) chain S residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 19) chain H residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 20) chain L residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 21) chain L residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 22) chain K residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 23) chain K residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 24) chain J residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 25) chain J residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 26) chain I residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 27) chain I residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 28) chain N residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 29) chain N residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 30) chain O residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 31) chain O residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 32) chain P residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 33) chain P residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 34) chain Q residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01398 source Swiss-Prot : SWS_FT_FI1 35) chain S residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 36) chain H residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 37) chain L residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 38) chain K residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 39) chain J residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 40) chain I residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 41) chain N residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 42) chain O residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 43) chain P residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 44) chain Q residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 45) chain R residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 46) chain M residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 47) chain T residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 48) chain G residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2

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