UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
|---|---|---|
Q0DTZ4 | MASPSSLLSWPHRAISLSFQPKNPSPSPATARVSVQDPPPPPSDANPSPGRSSNTSRYVWVNPNSPRAAGLARARAGSGRRARLAAAAAALAACEAGEAPVAAALEAAFPEPPSEQDAVIVLNTTSARPAAVVLALWWFLRNAEVRKEVILYNVALKALRKRRRWSDAEALWEEMLREGVQPDNATFSTVISCARACGMPGKAVEWFEKMPDFGCSPDMLTYSAVIDAYGRAGDAETALRLYDRARAEKWQLDPVICATVIRVHSSSGNFDGALNVFEEMKAAGVKPNLVVYNTVLDAMGRAMRPWVVKTIHRELVSQEAVPNKATYCCLLHAYTRARYGEDAMAVYRVMKDEVMDIDVVLYNMLLSMCADIGYVEEAEEIFRDMKASMDSRSKPDSWSYSSMVTLYSCTGNVAGAEGILNEMVEAGFKPNIFILTSLIRCYGKAGRTDDVVRSFAMLEDLGITPDDRFCGCLLTVAAGTPADELGKVIGCIDRSSAQLGAVVRLLVDAAAPSEPLREAAGELLGGARGVVRMPYCNCLMDLAVNLSQMEKACALLDVALRLGIYSNVQTRTQTQWSLHLRGLSVGAALTTLHVWMSDLYAALQAGDELPPLLGIHTGQGKNTYSYKGLATVFESHLKELDAPFHEAPDKAGWFLTTSVAARHWLETKKSAELVAV | Involved in translation and accumulation of chloroplast ATP synthase subunits. Belongs to the PPR family. P subfamily. |
Q41000 | MFRRATSTFLSRASATRRFSTDVATPATNSSFVEAWRKVSPNIDPPKTPLEFLKTRPPVPSTIPTKLTVNFVLPYSSQLAAKEVDSVIIPATTGEMGVLPGHVATIAELKPGVLTVQEGTDTTKYFVSSGFRFIHANSVADIIAVEAVPVNQLDRDLVQKGLQEFTQKLNSATTDLEKREAQIGIDVDSALNSALTG | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
P80085 | TSAEVPATAQGVTHALEGTQ | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
Q96253 | MASNAAVPFWRAAGMTYISYSNICANIVRNCLKEPHKAEALTREKVHFSLSKWADGKPQKPVLRSDTPEV | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the eukaryotic ATPase epsilon family. |
Q32PE5 | MVAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ. Belongs to the eukaryotic ATPase epsilon family. Extended N-terminus. |
P34539 | MVAWRAAGLNYVRYSQIAAQVVRQCTKGGANVKKPQATLKTTAWENGKMVSKSQ | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L) (By similarity). Belongs to the eukaryotic ATPase epsilon family. |
Q1ZXK8 | MAGQYWRAAGITYLQYANICGTHVRNCLKEPFRAAAKNREGFISNTVMYQNGKESSTIILNSELLQKELLVKKN | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L) (By similarity). Belongs to the eukaryotic ATPase epsilon family. |
Q53XU6 | MVAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAEKTSGSNVKIVKVKKE | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). Ubiquitous. The disease is caused by variants affecting the gene represented in this entry. Belongs to the eukaryotic ATPase epsilon family. |
B2G685 | MGGDALTFKLFGLTFNTTNIVSGLIIYAIVFFTLYGMSRKIQMKPTGAQNVFEWLVDFTNGIVRSQMPASEQGHYSFFAFVLFVFIFFANQFGLIFQFHWNGAEVLRSPTADPVVTLTLSLMVMVLAFAAGVAHNGLGGYLKGYTKPFTLMLPVNIIEDFANFLTLGLRIFGNIFAGELLMSLIANMAFSHGILTIIPGLFLELAWQGFSVFIGSIQAYVFVTLTTVYISRKISE | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
Q927V8 | MEEEFPTISLLGIDFNLSNILMITVTCVIVLLIAIICTRNLQRRPTGKQNFIEWVMDFVRGIINSNMDWKTGGRFHVLGITLLMFIFVANMLGLPFQIAINDEVWWRSPTADPIVTLTLAIMVLGLTHYYGIKMRGFKHYFVGTYFSPMKFLFPLKLVEEFANTLTLGLRLYGNIFAGEVLLTIIATQLAHMNIFVGVLAIIPALLWQGFSIFIGAIQAYIFTMLTMVYMSHKVSDEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
C1KYV2 | MEEEFPTISLLGIDFNLSNILMITVTCVIVLLIAIICTRNLQRRPTGKQNFIEWVMDFVRGIINSNMDWKTGGRFHVLGITLLMFIFVANMLGLPFQIAINDEVWWRSPTADPIVTLTLAIMVLGLTHYYGIKMRGFKHYFVGTYFSPMKFLFPLKLVEEFANTLTLGLRLYGNIFAGEVLLTIIATQLAHMNIFVGVLAIIPALLWQGFSIFIGAIQAYIFTMLTMVYMSHKVSDEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
Q71WP3 | MEEEFPTISLLGIDFNLSNILMITVTCVIVLLIAIICTRNLQRRPTGKQNFIEWVMDFVRGIINSNMDWKTGGRFHVLGITLLMFIFVANMLGLPFQIAINDEVWWRSPTADPIVTLTLAIMVLGLTHYYGIKMRGFKHYFVGTYFSPMKFLFPLKLVEEFANTLTLGLRLYGNIFAGEVLLTIIATQLAHMNIFVGVLAIIPALLWQGFSIFIGAIQAYIFTMLTMVYMSHKVSDEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
Q8Y4B6 | MEEEFPTISLLGIDFNLSNILMITVTCVIVLLIAIICTRNLQRRPTGKQNFIEWVMDFVRGIINSNMDWKTGGRFHVLGITILMFVFVANMLGLPLQIAVNDEVWWRSPTADPIVTLTLAIMVLGLTHYYGIKMRGFKHYFVGTYLSPMKFLFPLKLVEEFANTLTLGLRLYGNIFAGEVLLTIIATQLAHINIFVGVLAIIPAIIWQAFSLFIGAIQAYIFTMLTMVYMSHKVSDEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
A0ALL9 | MGEEFPTISLLGIDFNLSNILMITVTCVIVLLIAIICTRNLQRRPTGKQNFIEWIMDFVRGIINSNMDWKTGGRFHVLGITLLMFIFVANMLGLPFQIAINDEVWWRSPTADPIVTLTLAIMVLGLTHYYGIKMRGFKHYFVGTYFSPMKFLFPLKLVEEFANTLTLGLRLYGNIFAGEVLLTIIATQLAHMNIFVGVLAIIPALLWQGFSIFIGAIQAYIFTMLTMVYMSHKVSDEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
P14569 | MMTNLFSTFDPSTNLFNLSLNWTSTFLGLLLIPSMFWLMPSRINILWNKMNLNLHNEFKTLLGKNSFQGSTLILISIFIMMLFNNFMGLFPYIFTSTSHMTLTFSIALPMWMSFMLFGWINNTNHMFTHLVPQGTPNALMSFMVLIETISNVIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLTTSIMLFLIIGQMLLLILESAVAMIQAYVFSILSTLYSSEVY | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase A chain family. |
Q2I3F6 | MNEELSTFFYVPVGTMMLAIAFPAILLPTPNRLITNRWITIQQWLIQLIMKQLLSIHNTKGLSWSLMLITLTLFIGLTNLLGLLPYSFAPTTQLTVNLSMAIPLWTGTVVPGFRYKTKISLAHLLPQGTPMFLIPMIIIIETISLLIRPVTLAVRLTANITAGHSLIHLTGTATLTLSSIHSMTITVTFVTVILLTILELAVALIQAYVFALLISLYLHENA | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). Interacts with DNAJC30; interaction is direct (By similarity). Belongs to the ATPase A chain family. |
Q34946 | MMPDIFSSFDPYMFNTLFPLNSLFLVTNTAIILMIQSSFWVLNARTSAFKSPVNDTIFTQLSRTSTTHLKGLSTPLSTIFFMLVMINLMGLIPYMFSTSSHLVFTLSLGFPIWLSLMISTFAHSPKKSTAHFLPDGAPDWLNPFLVLIETTSVFVRPLTLSFRLAANMSAGHIVLSLMGIYCAAAWFSSVSSTALLILTAIGYILFEVAICLIQAYIFCLLLSLYSDDHAH | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase A chain family. |
O79551 | MTMNMFEQFMSPELLMIPTALLSMLVPVLLIHHNPKLLGNRMTTAIAWLLMTIMSNMTNQLTPSGQKWCQVLTSLLLMILLSNLLGLLPYTFTSTSQLSMNMAMAIPLWMATIITGMTKKPSITLAHMLPEGSPTPLIPFMIIIETISLLMRPLALGVRLTANITAGHLLMTMVSTTTLNFITSHITLSIMTYLLLFLLCILELAVACIQAYVFVLLIILYLQENT | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase A chain family. |
B1HM50 | MNHEAPLLEVGFLTFNKSTVMMLLVAAIIVFLIAFISTRSLKLKPTGMQNFMEWIMDFVKNIIKSNMDWKTGGRFHILGITLIMFIAVSNLLGLPFSIVYGHELWWKSPTADPTVTMTLATMILVLSHFYGVKMKGTGHYAGTFFKPMSFMFPLKLVEEFANTLTLGLRLYGNIYAGEILLGLLAGLASSGAVGFIGAIVPMMAWQGFSIFIGFIQAFIFTMLTMVYMAHKVSDDH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
B9E8F1 | MGHESPLYSLDLFGHEMIFDLSSMLMLTVTAAIVFLIAMLFTRNLSVRPHGKQNFIEWIFDFTRGIINSNMAWNKGGRFHFLAVTLLLFIFVANMLGLPFAIINGHTLWWKSPTADPTVTLTLSTLMVLLTHFYGVKMRGTGNYLKSFAQPVWFMVPFKIIEEFSSTLTLGLRLYGNIFAGEVLLGLLATLGTAGAAGMLGAAIPTLIWQGFSIFVGSIQAYIFVMLSMVYMSHKVSDDH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
A0LDW6 | MSAEAMHAAASAAPKMDPLHHFMVQKVVPIEIAGIDLSITNSTIWMWLAVAVAFLFMKWSFRGRAEDKLIPTKMQSLAEMTFTFVRQIVDQNIGGAEGRKYFPAIFTLFLLVLFCNLLGLIPGSFTPTSQLVVTATLALSVFFFATGLAIVKHGTGFIGFFVPSGVPPMLLILMVPIEIVSYLSRPVSLSVRLFANMTAGHTVLAIMFFFAATLPLGGLLMPAAFATVFTGFELFIGFIQAYIFTILTCVYINDALHLH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
Q2W028 | MANPIEQFKIQPLVPLKVGSVDISFTNSSAMMVLSICLITLFLTLSVRSRALVPGRWQSMAEVFYEFIAGMLRDNVGQEGRKYFPFIFSLFMFVLFGNLLGMMPIPVIGFTYTSHVIVTFAMALVVFVGVTVIGFARHGTHYLRMFFPHGAPIATAVILIPIELISYFSRPFSLAVRLFANMTVGHIILKVMGGFVVSLGAFYLIPGAVPFAFLSAITVLEFGIALLQAYVFTILSCIYLHDAIHMH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
P07925 | MERNGEIVNNGSIIIPGGGGPVTESPLDQFGIHPILDLNIGKYYVSFTNLSLSMLLTLGLVLLLVFVVTKKGGGKSVPNAFQSLVELIYDFVPNLVNEQIGGLSGNVKHKFFPCISVTFTFSLFRNPQGMIPFSFTVTSHFLITLALSFSIFIGITIVGFQRHGLHFFSFLLPAGVPLPLAPFLVLLELISHCFRALSSGIRLFANMMAGHSSVKILSGFAWTMLFLNNIFYFLGDLGPLFIVLALTGLELGVAISQAHVSTISICIYLNDATNLHQNESFHNCIKTRSQS | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase A chain family. |
Q38PR7 | MNEELSAFFDVPVGTMMLAIAFPAILLPTPNRLITNRWITIQQWLVKLIMKQLLSIHNTKGLSWSLMLITLTLFIGLTNLLGLLPYSFAPTAQLTVNLSMAIPLWTGTVILGFRYKTKISLAHLLPQGTPTFLIPMIIIIETISLLIRPVTLAVRLTANITAGHLLIHLTGTAALTLLSIHSMTITVTFITVVVLTILELAVALIQAYVFALLISLYLHESA | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). Interacts with DNAJC30; interaction is direct (By similarity). Belongs to the ATPase A chain family. |
Q65Q01 | MSGQTTSEYIGHHLQFLKTGDSFWNVHIDTLFFSVLAAIIFLAVFRSVAKKATSGVPGKLQCMVEILVEWINGIVKENFHGPRNVVAPLALTIFCWVFIMNAIDLIPVDFLPQLAGLFGIHYLRAVPTADISATLGMSLCVFALILFYTVKSKGFGGLVKEYTLHPFNHWSLIPVNFVLESVTLLAKPISLAFRLFGNMYAGELIFILIAVMYSANAAIAALGIPLHLAWAIFHILIVTLQAFIFMMLTVVYLSIAYNKAEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
Q0AMJ4 | MADTNPIKQFEVHEVFPFEAFGLNLAFTNSSYFMVLTTVLTIVLFMVAMSSRALVPNRAQSVAEIIYGFVADMVRSTAGQEGLRFFPFVFTLFIFILVANMLGMFPYFPAPGAHSFTITSHLIVTVALAMLVWLTVIIYGVFKNGFGFLKLFVPSGVPIFVLPLVVVIEIISFVSRPLSHSVRLFANMLAGHILLKVFAGFVVTLAAAWGGFGYLAGIAPLAMAVSLTALEFLVAFLQAYVFAMLTCIYLNDALHPGH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
A6W3T4 | MGIESPTASSYIKHHLQNLTYGQHPDGTWGLAHDAKEAADMGFWAIHVDTMAISIALGFLFLWLFRKAAKKISADTPSGLQNFVELMVEFVDGSVKETFHGKSKVIAPLALTIFVWVFLMNFMDLIPVDFLPATAQWIGVTLFGADPHHVYFKFVPTTDINATLGMSLSVFVLIVFYSIKVKGISGFVGELTLQPFGKWMIPFNLLLEGVGLLAKPVSLALRLFGNLYAGELIFILIAILPWGVQWALSVPWAIFHILIIVLQAFIFMMLTIVYLSMAHENH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
A1U7I0 | MAADTPVEYIKHHLTNLTYGKLPEGYERADGSVVQEATWTFARTGQEATDMGFMAIHVDTLGWSIAMGILFLGLFRFVANRVTEGTPSGLQNLIEMTFEFVQGIVRDVFHGKNPLIAPLALTIFVWILLMNILKLIPIDYIPSIAHALGLEYFKIVPTTDPNATFGMSIGVFLLILFYSFKVKGVSGFSKELAFNPFNHWIMIPFNLLLEILALIIKPISLALRLFGNMYAGEVVFILIALLPLWIQWTLNVPWAIFHILVIPLQAFIFTVLTVVYLSAAHEDH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
B0BVU2 | MTHSPLAQFDIKKLIDIKMFGFDVSFTNSSIYMLLASILALTYFYLAFYKRKLVPSRLQVSAEIVYNLVADMLNQNIGVKGRKFIPLVFSLFIFILFCNLLGMTPYSFTATSHIIVTFTLAILVFLIVTIVGFVKHGLRFLTLFLPHGTPLWLAPLMIVIELFTYLARPVSLSLRLAANMMAGHVLLKVIAGFTVSLMIYLKFLPIPIMVILIGFEIFVAILQAYIFTILSCMYLNDAINLH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
A8GQF6 | MTHSPLAQFDIKKLIDIKMFGFDVSFTNSSIYMLLASILALTYFYLAFYKRKLVPSRLQVSAEIVYNLVADMLNQNIGVKGRKFIPLVFSLFIFILFCNLLGMTPYSFTATSHIIVTFTLAILVFLIVTIVGFVKHGLRFLTLFLPHGTPLWLAPLMIVIELFTYLARPVSLSLRLAANMMAGHVLLKVIAGFTVSLMIYLKFLPIPIMVILIGFEIFVAILQAYIFTILSCMYLNDAINLH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
Q68XQ1 | MTNSPLIQFNIKKLIDIKMFGLDVSFTNSSIYMLLASTLALTYFYLAFYNRKLIPSRLQVSAEIVYNFVVDMLNQNIGIKGRKFIPLVFSLFIFILFCNLLGMTPYSFTATSHIIVTFTLALLIFLTVTIVGFIKHGMSFLTLFLPQGTPVWLAPLMIVIELFTYLAKPVSLSLRLAANMMAGHVLLKVIAGFTVSLMIYLKFLPIPLIVILIGFEIFVAILQAYIFTILSCMYLNDAINLH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
Q16AM8 | MADKAEGGGLVFKPMEQFEITALFGGDVTWYTPTNTALWMGFSIIAVVLLLVVGSSKRAVVPSRAQSVAELAYGFIYKMVEDICGKEGLKFFPYIMTLFMFIVCANFLGLIPSSFTPTSHFAVTVVLALAVFVTVTILGFVKNGTAFLSLFWVSSAPLALRPVLAIIEIISYFVRPVSHSIRLAGNVMAGHAVIKVFAGFAALTLVSPVAILGITAMYGLEVLVSFIQAYVFTILTCVYLKDALHPHH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a, b, b' and c. Belongs to the ATPase A chain family. |
Q1AVH3 | MEVTQEELRHEILHTWEAAREAWVIHLEIAGINLSINKPVWFLWLGAAITFLFMYVGARTLRDRPGAYQVLVEELFRFGRDMFGGQINEEGRKWFPYSLTLFIFLLVLNIIGLFPNSYPVTSNISFTATLALFTFVLTQYEGVRRNGLVTYLKSWAPADLPAKPLMYPIMWFLHLIQEFTKPLTLALRLYANILAGHLIIFVFLSLILYFGLPTAFVSVPFAVVFYAFEIFVAVIQAYIFAILTQVYIELAMFAEEAH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
A1AXU8 | MSATNEVITSGSYIKHHLQNLTYGQFPDGHWRFAHTTSEAKEMGFWAFHLDTLSISFILGALFLIFFYKVGKKMTSDTPSGAQNFIESVIDFINDNVRGSFNSQNPMVAPLALTTFIWIVLMNTMDLVPVDWLPYVAQQIGVWLGADPHHVFFKMVPTADPNATLGMSIGIFILIIYYSIKEKGAGGFAAELTFHPFGKMMLPFNLFLEGVNLIAKPVSLALRLFGNMYAGEMIFILIALLPFWVQWSLSLPWAIFHILIVLLQAFIFMTLVIVYMDMAHQKKH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
Q21DK2 | MASSEELTATGYIQHHLQNLTYGKLPAGYVRHNADGTHTELAANTWTFAHTAQEAKDMGFMAVHVDTLGWGIFLALLLGFIFRSAVKKAHTGKPSGLLSFVEFLVEGINSVVKDIFHHKNRLIAPMGLTIFSWVFMMNLMDLIPVDWLPMLAQVVTGDSHTFFKVVPTTDPNATLGMAFTVFALMIMFSIKEKGALGFVKELTCHPFFAPKKLWYLNILLIPVNTILETVALIAKPISLGLRLFGNMYAGEMIFILIALLFSVGLVMGFVGGVLQWAWAVFHILVITLQAFIFMVLTTVYMAMAHDNHDEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
B5EZ02 | MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
A9MJR3 | MASENMTPQDYIGHHLNNLQMDLRTFSLVDPHNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
Q57HX3 | MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
B5FN39 | MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
B5QVD8 | MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
B5RFV7 | MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
B4TAX8 | MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
B4SYD7 | MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
Q5PKW6 | MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
A9MXB2 | MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
C0Q2N8 | MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
B5BIP2 | MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase A chain family. |
Q35920 | MTLSFFDQFMSPTYLGIPLIAVALTLPWILFPTPSTRWLNNRLITLQGWFINRFTQQLLLPLNLGGHKWAVLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLMPIMPTVAILTSIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c (By similarity). Belongs to the ATPase A chain family. |
P80088 | TKXXEAPAPKGLKGNEMLKGIFLEVKKKFETA | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. |
Q6CFH9 | MSVAAARSSAVKVDWGKIVSSLGLTGATVSSLQAFRKRHEEAKKNAYELQNQPTTVDFAHYRKVLKNQKVVDEIEQHFKSFKPVTYDVSKQLKTIDAFEAKAIEDAKATEGKVNQEIGDLQKTLENIESARPFDQLSVDDVFKARPDLEKKIEEMVKKGRWSVPGYNEKFGSVVLM | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27373333). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (PubMed:27373333). Part of the complex F(0) domain and the peripheral stalk, which acts as a stator to hold the catalytic alpha/ATP1(3)beta/ATP2(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (PubMed:27373333). F-type ATP synthases have 2 components, the catalytic core F(1) and the membrane-embedded component F(0), linked together by a central stalk and a peripheral stalk (PubMed:27373333). The central stalk, also called rotor shaft, is often seen as part of F(1) (PubMed:27373333). The peripheral stalk is seen as part of F(0) (PubMed:27373333). F(0) contains the membrane channel next to the rotor (PubMed:27373333). F-type ATP synthases form dimers but each monomer functions independently in ATP generation (PubMed:27373333). The dimer consists of 17 different polypeptides: ATP1 (subunit alpha, 3 molecules per monomer, part of F(1)), ATP2 (subunit beta, 3 copies per monomer, part of F(1)), ATP3 (subunit gamma, part of the central stalk), ATP4 (subunit b, part of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP, part of the peripheral stalk), ATP6 (subunit a, part of the peripheral stalk), ATP7 (subunit d, part of the peripheral stalk), ATP8 (subunit 8, part of the peripheral stalk), OLI1 (subunit c, part of the rotor, 10 molecules per monomer), ATP14 (subunit h, part of the peripheral stalk), ATP15 (subunit epsilon, part of the central stalk), ATP16 (subunit delta, part of the central stalk), ATP17 (subunit f, part of the peripheral stalk), ATP18 (subunit i/j, part of the peripheral stalk), ATP19 (subunit k, dimer-specific, at interface between monomers), ATP20 (subunit g, at interface between monomers), TIM11 (subunit e, at interface between monomers) (PubMed:27373333, PubMed:25759169). The F-type ATP synthase complex is anchored in the mitochondrial inner membrane via the F(0) domain with the F(1) domain and the peripheral stalk extending into the mitochondrial matrix. Belongs to the ATPase d subunit family. |
D6VXS0 | MSLAKSAANKLDWAKVISSLRITGSTATQLSSFKKRNDEARRQLLELQSQPTEVDFSHYRSVLKNTSVIDKIESYVKQYKPVKIDASKQLQVIESFEKHAMTNAKETESLVSKELKDLQSTLDNIQSARPFDELTVDDLTKIKPEIDAKVEEMVKKGKWDVPGYKDRFGNLNVM | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j and k. Present with 6820 molecules/cell in log phase SD medium. Belongs to the ATPase d subunit family. |
Q47527 | MEQNLPSRITKLIKKSESGDFASSYQLYKVFGSKEYGVEPDEKMSDYFKELSAKQLEGGQLRVADIHLENYKGFESLIMDFSMKKNSTILVGNNGCGKSTILDAIQKGLTHLSSRLSTRSHNGDGIEKHELRKGQNYASIAINYDYMGIRFPMIIATTEPGYEDRAKSNYSGINELGSIFKTAHSINPNVSFPLIAMYTVERANDVSTRDIENSEEIKEAQIWDKFKAYNKSLTGKADFKLFFRWFKELIEIENSDNADITALRAEIRAKEKDLDNPLLKALLAENKNSETTKKLLEDHQNSLKVLKEKLNSYYSVNSKTLHTVEDAMYSFLPGFSNLKLQRAPLDLIVDKNNVSLSVLQLSQGEKTILALIADIARRLTLLNPNSVNPLDGTGIVLIDEIDLHLHPSWQQNIIPRLEKTFKNIQFIVTTHSPQVCHTIDSQNIWLLKNGQKFKAPKGVRGAISSWVLENLFEVAQRPPEDKYTKLLQEYKNLVFSEKYASEDARKLGATLSQHFGPDDETLVELKLEIEKRIWEDDFEKDQ | Probable ATPase component of antiviral defense system retron Ec83, composed of a non-coding RNA (ncRNA), a reverse transcriptase (RT), this protein and a putative HNH endonuclease. Expression of retron Ec83 confers protection against bacteriophage T2, T4 and T6. At multiplicity of infection (MOI) of 0.02 cultures slow growth when infected with T4 but do not collapse, at MOI 2 cultures enter growth stasis. |
Q751Q6 | MTPQIIPFFFMHQFTYGFLVILLTLLLLSYAFLSMILRLYLSRIYLSK | Belongs to the ATPase protein 8 family. |
B0FWC9 | MPQMAPISWLTLFFVFSITLVIFNIKNYFCFSYNSTETSQNLNIKQHKLNWKW | Mitochondrial membrane ATP synthase (F(1)F(O) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family. |
Q5JCK6 | MPQMAPISWLTLFFIFSITLVIFNMKNYFCFFYNSNESCQNLNIKQYKLNWKW | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family. |
Q3L6W9 | MPQLDTSTWSITITSVVLTLFIMFQLKILKSSFPNNPEPKSTPMLKTSMPWEKKWTKIYLPLSLPQH | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). Interacts with PRICKLE3 (By similarity). Belongs to the ATPase protein 8 family. |
P48895 | MPQLSPMNGLLIMFSVTLMLLIVLVINHFMLTPMASPLLASHLKTKKSGGEKLYY | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family. |
Q08076 | MPQLSPINGFVILCSISLMLLTLLINGHFMLKPISSLTTPKLKMAYIKKLYF | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family. |
O47871 | MPQLNPEPWLTTFLIVWISLIVILQPKIASLMLTSSPTPYKAMTIKTWPWPWT | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family. |
Q8HFZ6 | MPQLDMSPWPMVIMSMILTLFYITQLKMLNFTFHTTPSSKLTMSHKHKTTWELKWTKIYLPPSTYQ | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). Interacts with PRICKLE3 (By similarity). Belongs to the ATPase protein 8 family. |
Q8HG02 | MPQLDMSPWPMVIMSMILTLFYITQLKMLNFTFYNTPSSKLSMPHKHKTTWELKWTKIYLPPSMYQ | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). Interacts with PRICKLE3 (By similarity). Belongs to the ATPase protein 8 family. |
P50655 | MPQLNPAPWFSIMVMTWLTLALLIQPKLLTFTTTNPPSKKPSLITKPTPWAWPWT | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family. |
P34836 | MPQMAPINWLILFIVFSITLVVFNILNYFCFFYTPLKTSQSLNIKFNKLNWKW | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family. |
P33506 | MPQMAPINWLILFFIFSITLVIFNILNYFCFSYTPMKTSQSLNIKFNKLNWKW | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family. |
Q00276 | MPQMMPMKWFLIYFIYLLIFYLFIMLINSMLIKTKINKETLKIKLKKWNWFW | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family. |
Q9MJC0 | MPQLEFTWWIINFFIVWTADFTLLIVLSIPNLSTPTTLSKQLDINKSHVTWQWS | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family. |
O99598 | MPQLDTSTWFITILATILTLFIIMQLKISTYYYHSNPEPKTTKMTKSLIPWEIKWTKIYSPLSLPLR | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). Interacts with PRICKLE3 (By similarity). Belongs to the ATPase protein 8 family. |
Q37707 | MPQMMPLPWIMVFLVSMALLWAIMTMVFFLYQPRSVSSAKGFSDRTVYLNWKW | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. Belongs to the ATPase protein 8 family. |
Q75G38 | MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALIQGVSRNPSMKDTLFQFAILGFAISEATGLFCLMISFLLLYGV | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 18 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i, j and k. Belongs to the ATPase C chain family. |
P14571 | MLEGAKSIGAGAATIASAGAAIGIGNVFSSLIHSVARNPSLAKQLFGYAILGFALSELIALFALMMAFLILFAFRFFSKKGKLAGAPV | This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase. ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
Q08366 | MLEGAKSIGAGAATIASAGAAIGIGNVFSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLILFVF | This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c (By similarity). Belongs to the ATPase C chain family. |
Q9B8D5 | MQLALAAKYIGASIATLGLGGAAIGIALVFVALINGTSRNPSLRSTLFPQAILGFALSEACGLFCLMISFLLLYAV | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
Q85Q98 | MQLALAAKYIGAGISTIGLIGAGIGIGIVFAALINGVSRNPSLKDTLFSYSILGMALSEATGLFCLMISFMLLFAV | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
P48880 | MNVTLQSAKMIGAGLATIGLTGVGAGVGIVFGSLVMAYARNPSLKQQLFGYTILGFALTEAVALFALMMAFLILFT | This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
Q36852 | MQLVLAAKYIGAAISTIGTLGAGIGIAIVFAALINGTSRNPSLRNTLFPFAITGFALSEATGLFCLMVSFTLLYGV | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
A9RAH4 | MQLALAAKYIGASMATLGLGGAAIGIALVFVALINGTSRNPSLRATLFPQAILGFALAEACGLFCLMMSFLLLYAV | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
Q2LCR3 | MKNIVKIEQLELASAVVELGKKVGAGLAAIGLTGAGAGVGIVFAAFILAVGMNPNLRGELFKLAMLGFALSEAVGLLALMMSFLILYS | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c (By similarity). Belongs to the ATPase C chain family. |
Q37315 | MKNIVKIEQLELASAVVELGKKVGAGLAAIGLTGAGAGVGIVFAAFILAVGMNPNLRGELFKLAMLGFALSEAVGLLALMMSFLILYS | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c (By similarity). Belongs to the ATPase C chain family. |
Q5BCV6 | MAASRVFAQRLASTMKVARPAARIQARTLTTQRMATPFQTIKRQQPSMIQASARQAFAARRQYSSEIADAMVQVSQNIGMGSAAIGLGGAGIGIGVVFGSLLLAVSRNPALRGQLFSYAILGFAFVEAIGLFDLMVAMMCKYV | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
P17254 | MLEGAKSIGAGAATIASAGAAIGIGNVLSSSIHSVARNPSLAKQSFGYAILGFALTEAIASFAPMMAFLISSVIPIKESKKEG | This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
Q6DN63 | MQLVLAAKYIGAGISTIGLLGAGIGIAIVFSALIQGVSRNPSLKDTLFPFAILGFALSEATGLFCLMISFLLLYAV | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
P00840 | MLEGAKLIGAGAATIALAGAAVGIGNVFSSLIHSVARNPSLAKQLFGYAILGFALTEAIALFALMMAFLILFVF | This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
Q37550 | MLEGAKSIGAGAATIASAGAAIGIGNVFSSLIHSVARNPSLAKQSFGYAILGFALTEAIASFAPMMAFLISSVFRSVSRVTI | This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c (By similarity). Belongs to the ATPase C chain family. |
P26855 | MLEGAKLIGAGAATIALAGAAVGIGNVFSSLINSVARNPSLAKQLFGYAILGFALTEAIALFALMMAFLILFVF | This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
Q7S5B4 | MASTRVLASRLASQMAASAKVARPAVRVAQVSKRTIQTGSPLQTLKRTQMTSIVNATTRQAFQKRAYSSEIAQAMVEVSKNLGMGSAAIGLTGAGIGIGLVFAALLNGVARNPALRGQLFSYAILGFAFVEAIGLFDLMVALMAKFT | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase C chain family. |
P14572 | MLEGAKLMGAGAATIALAGAAIGIGNVFSSLIHSVARNPSLAKQLFGYAILGFALTEAIALFALMMAFLILFVF | This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. The stop codon at position 75 is created by RNA editing. Belongs to the ATPase C chain family. |
Q7JAI7 | MLEGAKLIGAGAATIALAGAAVGIGNVFSSLIHSVARNPSLAKQLFGYAILGFALTEAIALFALMMAFLILFVF | This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. The stop codon at position 75 is created by RNA editing. Belongs to the ATPase C chain family. |
P23413 | MELSPRAAELTNLFESRIRNFYANFQVDEIGRVVSVGDGIAQVYGLNEIQAGEMVLFANGVKGMALNLENENVGIVVFGGDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDAMGVPIDGRGALSDHEQRRVEVKAPGILERKSVHEPMQTGLKAVDSLVPIGRGQRELLIGDRQTGKTTIAIDTILNQKQINSRATSESETMYCVYVAIGQKRSTVGQLIQTLEEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSSKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVPKQPQYAPLPIEKQILVIYAAVNGFCDRMPLDRISQYEKAIPNSVKPELLQALKGGLTNERKMEPDAFLKERALALI | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
P22201 | MELSPRAAELTNLFESRIRNFYANFQVDEIGRVVSVGDGIAQVYGLNEIQAGEMVLFANGVKGMALNLENENVGIVVFGGDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDAMGVPIDGRGALSDHEQRRVEVKAPGILERKSVHEPMQTGLKAVDSLVPIGRGQRELLIGDRQTGKTTIAIDTILNQKQINSRATSESETMYCVYVAIGQKRSTVGQLIQTLEEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSSKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVPKQPQYAPLPIEKQILVIYAAVNGFCDRMPLDRISQYEKAIPNSVKPELLQALKGGLTNERKMEPDAFLKERALRLI | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
P18260 | MEFSPRAAELTTLLESRISNFYTNFQVDEIGRVVSVGDGIARVYGLNEIQAGEMVEFASGVKGIALNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRSTSESETLYCVYVAIGQKRSTVAQLVQILSEANAMEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVIPITDGQICSETELFYRGIRPAINVGLSVSRVGSAAQLKTMKQVCGSSKLELAQYREVAALAQFGSDLDAATQALLNRGARLTEVPKQPQYAPLPIEKQILVIYAAVNGFCDRMPLDRISQYERAILKSIKTELLQSLLEKGGLTNERKMEPDTFLKECALPYTI | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
P05494 | MEFSPRAAELTTLLESRMINFYTNLKVDEIGRVVSVGDGIARVYGLNEIQAGEMVEFASGVKGIALNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGKGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRGTNESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSMLVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSSKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVPKQPQYEPLPIEKQIVVIYAAVNGFCDRMPLDRISQYEKNILSTINPELLKSFLEKGGLTNERKMEPDASLKESALNL | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
P26854 | MNKLAGAELSTLLEQRITNYYTKLQVDEIGRVVSVGDGIARVYGLNKIQAGEMVEFASGVKGMALNLENENVGIVIFGSDTAIKEGDIVKRTGSIVDVPVGKGMLGRVVDALGVPIDGKGALSAVERRRVEVKAPGIIARKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQINAQGTSDSEKLYCVYVAIGQKRSTVAQLVKILSEAGALEYSIIVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQSVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKMSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYRGSRPAINVGLSVSRVGSAAQLKAMKQVCGSLKLELAQYREVAAFAQFGSDLDAATQYLLNRGARLTEILKQAQYSPIPIEKQIVVIYAAVKGYLDQIPVALITHYEQELLKSIDPGLLSAIVQQKNITEQISSQLATFCQKFTQSFLATHQS | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
P05495 | MELSPRAAELTSLLESRISNFYTNFQVDEIGRVVSVGDGIARVYGLNEIQAGEMVEFASGVKGIALNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQLNSRATSESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVIPITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKTMKQVCGSSKLELAQYREVAALAQFGSDLDAATQALLNRGARLTEVPKQPQYAPLPIEKQILVIYAAVNGFCDRMPLDRISQYERAIPNSVKPELLQSFLEKGGLTNERKMEPDTFLKESALAFI | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
P05492 | MEFSPRAAELTTLLESRITNFYTNFQVDEIGRVISVGDGIARVYGLNEIQAGEMVEFASGVKGIALNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKSLLGRVVDALGVPIDGRGALGDHERRRVEVKVPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRATSESETLYCVYVAIGQKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSLKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEILKQPQYAPLPIEKQIIVIYAAVNGFCDRMPLDRISQYERAIPQSVKQELLQSLVEKGGLNNERKIEPDAFLKENAKPYIKG | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
Q7JAI5 | MEFSPRAAELTTLLESRMTNFYTNFQVDEIGRVVSVGDGIARVYGLNEIQAGEMVEFASGVKGIALNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGKGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRGTNESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSLKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVSKQPQYEPLPIEKQIVVIYAAVNGFCDRMPLDRISQYEKAILSTINPELLKSFNEKGGLTNERKIELDAFLKQTAKEIN | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
P05493 | MEFSVRAAELTTLLESRITNFYTNFQVDEIGRVVSVGDGIARVYGLNEIQAGELVEFASGVKGIALNLENENVGIVVFGSDTSIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRATSESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSLKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVLKQPQYAPLPIEKQILVIYAAVNGFCDRMPLDKIAQYERDILSTIKQELLQSLKGGLTGERKIEPDAFLKEKALSLI | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
P24459 | MEFSSRAAELTTLLESRMTNFYTNFQVDEIGRVVSVGDGIARVYGLNEIQAGEMVEFASGVKGIALNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRATSESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQACGSLKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVLKQPQYAPLPIEKQILVIYAAVNGFCDRMPLDKIPQYERDILTTIKPELLQSLKGGLTSERKIELEKFLKEKAKNYTL | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
M1FPH1 | MEFSVRAAELTTLLESRITNFYTNFQVDEIGRVVSVGDGIARVYGLNEIQAGEMVEFASGVKGIALNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRATSESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSLKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVLKQPQYAPLPIEKQILVIYAAVNGFCDRMPLDKIPQYERDILTTIKPELLQSLKGGLTSERKIELEKFLKEKGGTYYI | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
P80082 | MEFSPRAAELTTLLESRISNFYTNI | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
P12862 | MEFSPRAAELTTLLESRMTNFYTNFQVDEIGRVVSVGDGIARVYGLNEIQAGEMVEFASGVKGIALNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGKGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRGTNESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSSTALPVIETQAGDVSAYIPTNVISITDGQICLETDVFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSSKLELAQYREVAAFAQFGSDLDAASQALLNRGARLTEVPKQPQYEPLPIEKQIVVIYAAVNGFCDRMPLDRISQYEKAILSTINPELQKSFLEKGGLTNERKMEPDASLKESTLPYL | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Peripheral membrane protein. Belongs to the ATPase alpha/beta chains family. |
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