UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
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Q0PC33 | MENIIARRYAKAIASRADINDFYQNLCILNSAFVLPKFKNIIESNEIKKERKMEFLDSFFDIKNSSFQNFLRLLIENSRLECIPQIVKELERQKAFKENIFVGIVYSKEKLSQENLKDLEVKLNKKFDANIKLNNKISQDDSVKIELEELGYELSFSMKALQNKLNEYILKII | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
A1VXI7 | MENIIARRYAKAIASRADINDFYQNLCILNSAFVLPKFKNIIESNEIKKERKMEFLDSFFDIKNSSFQNFLRLLIENSRLECIPQIVKELERQKAFKENIFVGIVYSKEKLSQENLKDLEVKLNKKFDANIKLNNKISQDDSVKIELEELGYELSFSMKALQNKLNEYILKII | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B0TI53 | MLTGAVARRYAQALLEIGIQTKTLDALEGELGRFVEMIGHPELQRFLFHPSIVVAEKKDLVGRLLATGAFSETARAFILLVIDRRRESYFADIFREFVRLANKVRNIEEARVTSAVELAPEQVERLRSQLAAATGKAIVLRMAVDPDLIGGLVVAFGDRIIDGSVAGKIRDLRESLLRSPLPSLS | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains (By similarity). Belongs to the ATPase delta chain family. |
A4GAH2 | MAELATIARPYAEALFRVAKAADLNGWSELVSEMAQVAAHPDVYALAHNPKISDDVISSAFISALKSPVGAEAKNFINMLVQNDRLTLLPEIATQFHALKNAQEGAADAEIVSAFELSAAQLTELVATLEKKFGRKLNPTVAVDSALIGGVRVVVGDEVLDTSVRAKLQQMQVALTA | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B2XT89 | MSTNSRAGDAYAYALLKVLFNETKDFDSFSDLVGDVLDFVTIFNTCPSIEEFFANPTYSPIQKKQFLYDFFGRSLNPILMSFLYLLCDTKRIIYISSIISIFLETLLKNTNSHIVEVQTPTGKDYKLDISKLETTLSGWFNKIQKNNDEAVNFLNFDESLVIFTVKEVPGLLGGFRLNFVTDSKVIDFSIAGKIKRLAAVLNY | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase delta chain family. |
B2XTP5 | MSTNSRAGDAYAYALLKVLFNETKDFDSFSDLVGDVLDFVTIFNTCPSIEEFFANPTYSPIQKKQFLYDFFGRSLNPILMSFLYLLCDTKRIIYISSIISIFLETLLKNTNSHIVEVQTPTGKDYKLDISKLETTLSGWFNKIQKNNDEAVNFLNFDESLVIFTVKEVPGLLGGFRLNFVTDSKVIDFSIAGKIKRLAAVLNY | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase delta chain family. |
B0UWG8 | MSELTTIARPYAKAVFDFAVEQSEKDKSAVEKWTNMLEFLSELIRHDKVQSYLTSTSSTFKLADTVILICGEQLDQYGQNLVRLMAENKRLAVLPAVFNEFKSYVEEYKSLSQVEVVSAQQLNDVQQQKIITAMEKRLARKVILNCRIDSSLIAGAIIRTNDFVIDGSCRGQINRLANELRL | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q6FG90 | MLPAALLRRPGLGRLVRHARAYAEAAAAPAAASGPNQMSFTFASPTQVFFNGANVRQVDVPTLTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSIAVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQAELVGTADEATRAEIQIRIEANEALVKALE | 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:29478781). 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 (PubMed:1531933). 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). Disease susceptibility is associated with variants affecting the gene represented in this entry. Belongs to the ATPase epsilon chain family. |
Q31DL7 | MAELITIARPYAEAAFEVAKEEGKLVEWSEQLANLSAIVSDETMTAYMVNPSVTSEDVLKLLVDVMDSNLNSEVKNLLNVMAENKRLDALSEVAEVFEELKATEDKRVRATVISARKATVEQKKKLSAALNAKFDAEVEITYEEDPSLISGIKIKVGDWAIDGSALSQLNKLGAAIAQ | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B4U990 | MKVNKELARKLSKKIVFSVPKDKESLSAVSDFLGLLGVLYKKEPKFRDFVLSPFVSNEQKKLFIKSLIQKGNIPKEIEFFVDELIDLNLLRIVGEIKRLFDYESEKILSIYKGKLIFAKEPVKELVDEIIQRVEKVLNRKIEPEISVNEALIGGFELRLSGLVLDTSVRSVLQNLSNKVKSL | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q0C0Z7 | MIQTSETAQRYARALFELAQDKGDLATIHKDFRAFAALIKTSADLRKLLDSPAFSRDVKVSALAEIAKKAGYSPLFGKFLGTMATNGRANDILGAEFAFDQFYAKQRGVQRAIVRTAKEMTGAEKSRIESLLARVVGGDVELTSEVDPSLIGGIQLRLGSKLVDASVAKKLERMNTVMKGA | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q5QZI3 | MSELTTVARPYAKAAFDFALEQGALDKWAEMLSFAAAVAQDETIASFLSSSSTVGKTTEVFLGVCGDELDDNAKNFVKVLAENERLPVLPAVSELYQTLRAEHDKEVTVDVKSAVKLLKAQQTALIKALEKRLQRKIKLNCSVDKSIIGGLVIEAGDTVIDGTLRGKLDRLAYALQS | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q8KRV1 | MIEAQVGKRYAEAIYGIAEANNKVKELYDSLNIVMELYKGDKEFKNLVDHPLVKKEEKKEFINKVFSEFEKFSLDILCYLVEKNRLSYIRGVVAEYLKIYYTKNRIVDVEATFAIEPSEKQKAKLIEKLEKKTGKKVNLVIKINKAIIAGGIIKIGDEIIDGSVRRQLDTVARG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. The ATPase of I.tartaricus is of special interest because it uses sodium ions instead of protons as the physiological coupling ion. Belongs to the ATPase delta chain family. |
A6T473 | MAELATIARPYAEALFRVAKAADLNSWANLVSEMAQVAANPDVYALAHNPKVSDDLISSTFISALKSPVGAEAKNFINMLVQNDRLTLLPEIATQFHALKNAQEGAADAEIVSAFELSSAQLTELVATLEKKFGRKLNPTVTVDGALIGGVRVVVGDEVLDTSVRAKLQQMQVALTA | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q28TJ9 | MSEPASISTGIAARYATAMFELAEEAKALPALEKDVDALDAALSESADLRDLIHSPIYGRDEASAAIGGVADAMKLQDMTGNTLRLMASKRRLFVLPALLSELRERIADHKGEVTAEVTSAKALTKTQLDKLTKSLKAQVGKTVTVKETVDENIIGGLIVKIGSKMIDTSVRSKLNALQNTMKEVG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase delta chain family. |
A6W7G6 | MSGELDAGVAKASLAAAQQVLDVQLSAEGADAGKTGEDLFAVTSLLDSSVGLRRALTDPSRSGAAKAEFVRRTLSGRITPAALETVVALASARWAAGRDLSDATERLAVVAVVTQAERSGHLDALEDELFRFARTVAGSPALRDALADRTAPDANRASLAARLLLGKASPETVQLARRAASSSRGMRAERLLEEWVEVVAKRREQLVAHVVSATPLTDAQRERLAATLSRQYGRAIRVNLDVDPHLVGGLRVSVGDDVIDGSISTRLDEARRRLAG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B5XZM1 | MSEFVTVARPYAKAAFDFAVEHNSVERWQDMLAFAAEVTKNDQMAELLSGALAPETLSEAFIAICGEQLDENGQNLIKVMAENNRLKVLPDVLEQFIHLRAASEAIAEVEVISANQLSDEQLARIVSAMEKRLSRKVKLNCKIDKSVMAGIIIRAGDMVIDGSVRGRLDRLADVLQS | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
A6TG39 | MSEFVTVARPYAKAAFDFAVEHNSVERWQDMLAFAAEVTKNDQMAELLSGALAPETLSEAFIAICGEQLDENGQNLIKVMAENNRLKVLPDVLEQFIHLRAASEAIAEVEVISANQLSDEQLARIVSAMEKRLSRKVKLNCKIDKSVMAGIIIRAGDMVIDGSVRGRLERLADVLQS | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q6CJZ5 | MFRLSAARTLAKSVNTVVAKRTYAEAADGALKLQFALPHQTLFSGTPVTQVNLPAKSGQIGILANHVPTVEQLVPGVVEVLEGSSSKKFFVSGGFATVQPDSTLAITSVEAFPLESFSPENVRSLLAEAQKNVSSADEVAAAEAAIQLEVLEALQAALK | 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. |
B2GLY7 | MAEASNEPYRPLTVDVDRWAAAATPEIAHQLFEIVDIVDANGALRRALTDPSRSGEDRARLVHTLLDGRANEVAVDIVAELASQRSATERQLGDGIERTAVLVAAAAAENRGGGHALEALVDDLIRFKSMLDRSADVQRAFSDSRASAEAKVTLARRLAHTESDEAALLIERAVSAPRGSLPGRLLEQFAQWVADRQQRWIARVETARPLGEEQLARLQDGLNRLYGRDLKLTTETNPSLVGGLRVQVGEEIIDGSLTHRLGQLQQRIGA | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q1IIG5 | MASVTIRYANALADVVLSNRLDVTTAVRDLNNIVSMTIESEDLRKVWENPSIAVAQKRAILDGLVGMVGTPRIIRNFVAVLIDHQRVPLLPRIARQFELELNHRMGFADAEVTSVHELSAQDRQMIEQQIAKVVGKSVRARYKTNATLLGGAIIRVGSTVYDGSIKGQLAKIKEQLSAS | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q5FKY3 | MALSREEVAARYGTALFGYAQDNKVLDTVYDEMMALKKAAIANPKFISVLSDPILSSKDKKSILTAVEKDFSDEVQGFLNLLLEYNRFADLIDIIDQFSLLYDNENKIASGTATTAVKLDDDQLERLSESFAKKYDLNAVRLENKVDPSILGGVILQVKDRVIDGSVKNKLKKIRAQIIDEN | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. Increases 2-fold following exposure to low pH. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. By low pH. Belongs to the ATPase delta chain family. |
P35434 | MLPAALLRHPGLRRLVLQARTYAQAAASPAPAAGPGQMSFTFASPTQVFFDGANVRQVDVPTLTGAFGILASHVPTLQVLRPGLVMVHAEDGTTTKYFVSSGSVTVNADSSVQLLAEEVVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE | 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) 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 ATPase epsilon chain family. |
A9WNC5 | MAGISSDSRAKVLAELESVLPTATAQLARELFSVLAVVDSSAGLRRALTDPSREGKDKAALLSSLVRGKVSAQAEQIVDSLAKERWASARDLGDALETVAATVAIAVAENEAPGAEGLEKLENDLFVFNQTVAANHQVQRALSEPQASAEAKQKLASALVPGASQVAELLIGQAVAAPRGARPAKLVEQFATLAAARQQRWIATVTVGQALNKNQEARLSAGLNNLYGRDLKVNISVDPTLIGGVRVRVGDEVVDASVVNRLGELRRQLAG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
A6MVW5 | MSSKNVKVAKPYADAFIEIANKGSVINDLNCIATALSESKDLQKAIANPLVSSAAKKDIIKSIFAGNVDENTVKFMMVLCDRGRIEYLDAIAETALILAYKQASIEMAYVASSVKLSSAQTEALVDKLKAMTKADQIKLELKVDESLIGGFKVQIGSRIIDTSVQNQLKQLSSYLGASVA | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase delta chain family. |
B3PQ71 | MPVADTSQLTSGVAERYASSLFELALEHGAVDSVTADLDRFQAMLDESAELKRFVASPVFSAEDQLKAIVAISERAGISGFFANFLKVVARNRRLFALPGMIRAFRLIAANHRGEISAEVISAHALSQAQETELKAALKSVTGKDVTISVTVDPSILGGLIVKVGSRQIDTSLRTKLSTLKLALKEVG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q2K3G7 | MPVADTSQLTSGVAERYASSLFELALEQGAVDSVTADLDRFQAMLDESAELKRFVASPVFSAEDQLKAIIAISERAGISGFFANFLKVVARNRRLFALPGMIKAFRVIAANHRGEISAEVTSAHALTAEQENELKAALKGVTGKDVAIAVTVDPSILGGLIVKVGSRQIDTSLRTKLSTLKLALKEVG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q1MAY9 | MPVADTSQLTSGVAERYASSLFELALEQGAVDSVTADLDHFQAMLDESADLKRFVASPVFSAEDQLKAIVAISEKAGISGFFANFLKVVARNRRLFALPGMIKAFRIIAANHRGEISAEVTSAHALSQAQETELKVALKGVTGKDVTIAVTVDPSILGGLIVKVGSRQIDTSLRTKLSTLKLALKEVG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q98EV5 | MAQSSSPISGVAERYAGSLFELALQANSVAKVESDLNSFEAMLAGSSDLTRLINSPVFSGEEQAKAIAAIADKAGITGLTGNFLRVVARNRRLFAVPGMIKAFRQIAAEHRGETAAEVTSAHELTAAQQTELKAALKSVAGKDVAISVTVDPSLLGGLVVKIGSRQIDTSLKTKLNSLKLALKEVG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B5ZSP0 | MPVADTSQLTSGVAERYASSLFDLALEQGAVDSVTADLDRFQAMLDESADLKRFVASPVFSAEDQLKAIVAISEKAGISGFFANFLKVVARNRRLFALPGMIKAFRIIAANHRGEISAEVTSAHALSQAQETELKVALKSVTGKDVTIAVTVDPSILGGLIVKVGSRQIDTSLRTKLSTLKLALKEVG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q92LK5 | MPVADTSQLISGVAERYASSLFELALDAGSIEAVGADLTRIQALIDGSDDLKRLIVSPVFSADDQFKAISALVEKFGFSGLVGNFLKVVARNRRLFVLPGIIKAFRLLAARHKGEITADVTSAHALTLAQEIELKAALKGVTGKDVAVNVTVDPSILGGLIVKVGSRQIDTSLRTKLSTLKLALKEVG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
A5V3X2 | MENSGGIQASLSGRYATALFGLARDEKAIDAVSASLQSLKAALTESDDFRRLTTSPLVSRDEAMKAVAATAASLGIDPLTTKFLGVLAQNRRLGQLGAVIRSFGTLSARHRGETTAEVTSAHPLTATQVKALKAKLKTQLDRDVAVDLTVDPSILGGLIVKIGSRQIDGSIRSKLNSLAIAMKG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q7UFB8 | MVKLPSLKFLRRSTDETPNVSETASHSTVLDVGAEKLGKTYARALLAATQADGSTDAVVSDLNAICDEALLHNPKLQLAFQSPQIDADEKCRVVDRLFGGNSHPTLIKLMKVMAKRGRLGYLVAVRDAAVDLFDEAAGRVVAEVRTAVPMTEQLRGEVTQQLSSRFGKTVRLRESVDTELIGGMVIRVGDTVFDSSVASRLDKLGKSAAAGFARQLIEQSDRFSSSS | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
P72244 | MSEPASISAAIAGRYATAIFDLAQEAKGIDALSADVDALTAALAGSAELRDLISSPVYTREEQGDAIAAVAAKMGLSAPLANGLKLMATKRRLFALPQLLKGLAAAIAEAKGEMTADVTSATALSAAQAEKLAATLAKQTGKTVKLNVAVDESLIGGMIVKLGSRMIDTTVKAKLASLQNAMKEVG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B6IPC9 | MATEGTGVSGLAARYATALFELADENKALDQTAQDLALLKQLMAESADLRRVVRSPLLSRSDQARAMDAVLAQVDVSGLVRQFVGLVARNRRLFALSGMIDGFLAELARRRGEQTARVVAARPLSQEQLDALTDALRRALGSKVSVDLRVDPSLIGGMVVKVGSRMIDSSVRTKLTKLKLAMKGVG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase delta chain family. |
Q0SGP6 | MYAASREALTQTRAALSSALGSVSAGAATAAAAQIGAELFSVVEILDEQRTLRSALSDTSTPGNVREGLAEQVFGGKVSAETLAVLKAAVGQDWSVTSDLLNSLVLVGRESLLKAAADQGQLDAVEDELFRLGRIVAGNPKLEQSLSDRSVPAKRKRELLSKLLYGKVTAVAEALATQAVGRLKNSAPADAFDELSNLAAAQREAVVAKVRSSAPLSSEQSDRLTATLTRTYGKPVTVHVEVDPELLSGLVVRVGDEVIDGSGAGRLAALRKSLK | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
C1AW02 | MSTMYAASREALTQTRAALSSALGSVSAGAATAAAAQIGAELFSVVEILDEQRTLRSALSDTSTTGSVREGLAERVFGSKVSAETLAVVKSAAGQDWSVTSDLLNSLVLLGRESLLKAAADQGQLDAVEDELFRLGRIVAGDPKLEQSLSDRSVPAKGKRDLLSKLLYGKVTAVSEALATQAVGRLKNSAPADAFDELSNLAAAQRKAVVAKVRSAAPLSSEQSDRLTATLTRTYGKPVTVHVEVDPELLSGLVVRVGDEVIDGSGAGRLAALRKSLK | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q2J3I1 | MASEDPSVSGVSGRYATALFELARDEKVVDAVTADLDKFKAMLADSPDLLRLVRSPVFGAEAQAKALGAVLDKAGITGISANFLKLLAANRRLFVVADVIRAYRALVAKFKGEATADVTVAETLGDKNLEALKAALKAVTGKDVTLNINVDPAIIGGLVVKLGSRMVDSSIRTKLNSIKHAMKEAG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase delta chain family. |
Q07UZ2 | MAAENPSVSGVAGRYATALFELARDQKSVDAVKADLDRFKAMLAESPDLTRLVRSPVFSADAQGKALVAVLAKAGIGGIAANFLQLLNANRRLFAVHDVIRAFGALVAKFKGEATADVTVAEPLNDQNLDALKSALKSVTGKDVTLNVNVDPAIIGGLVVKLGSRMVDSSLRTKLNSIKHAMKEAG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase delta chain family. |
Q6NDC9 | MASEDPSVSGVSGRYATALFELARDEKSIDAVTADLDKFSAMLAGSPDLVRLVRSPVFASEVQGKALAAVLDKAGITGISANFLKVLAANRRLFVVADVIRAYRALVAKFKGEATADVTVAEKLSDKNLEALKAALKSVTGKDVALNINVDPAIIGGLVVKLGSRMVDSSLRTKLNSIKHAMKEAG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase delta chain family. |
Q21CY4 | MAAENPSVSGVSGRYATALFELARDEKAVDAVKADLDRFKAMLADSPELTRLVRSPVFSAETQSKALAAVLDKAGFAGTTAKFLKVLTANRRLFTVTDVIRAYGALVAKFKGEATADVTVAEPLSEKNLDALKTALKSVTGKDVALNVNVDPAIIGGLVVKLGSRMVDSSLRTKLNSIKHAMKEAG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase delta chain family. |
Q13DP5 | MASEDPSVSGVSGRYATALFELARDEKVIDAVKADLDKFSAMLVESPELLRLVRSPVFGAEAQTKALGAVLDKAGIAGISANFLKLLAANRRLFVVADVIGAYRALVARFKGEATADVTVAETLSDKNLEALKLALKSVTGKDVTLNINVDPAIIGGLVVKLGSRMVDSSIRTKLNSIKHAMKEAG | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase delta chain family. |
Q7MGH7 | MADFTTIARPYAKAAFDFAVEKGQLDQWGQMLSFAAEVAQNEQISELLSGSMSADKLAELFIAICGEQVDEFGQNLLKVMAENGRLAALPDVCTLFFVLKKEHEKEIDVEVISATELSDEQCANISQKLEQRLERKVKLNCSVDEALLGGVIIRAGDLVIDNSARGRLNRLSDALQS | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q8D3J6 | MTIYEIKSYLSRPYAEAAFKFANENNIVDDWIYMIEEICKILKNIKIYSLSSFILKKNKNFLFESIKNNFDVYFNNFVKIIIENNRLIIFPEILNQFINLKNDQNNIENITIISKYKLDKKILNKIEKKIKSLIFKEIKINIKIDKSIIGGYIIKSKNFLIDNSIKNKLYRFSEYL | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q73HB1 | MKKTQYNNLVSSYARVLFHVSGSRLGIIRKEVEFLLAFFKDQRDVFVYLSHPMISFAHKKEVMLSINEHLSENLVKFIMVIFANKRSSLLILILEKFLSLARENENEFEITIKSAETLKESDIKIITESLSFLGKIIKVSNVVDPSILGGFVVRYGFNLIDASLKSYLDRLVDLSKMEILKVRNFV | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B3CN52 | MNMKNNNLVSSYARALFHVSGSRLGIIRKEVEFLLAFFKDQDVFVYLSHPMVSLLHKKEAILSIKENLSENLVKFIMVTLANKRSRLLILILEKFLNLVRESENELEITIKSAEILKKPDIKIITESLNFLGKIIKVSHVVDPSILGGFVVRYGFNVIDASLKSYLDRLVDLSKMEMLKIRNCI | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q7MA21 | MRELVAKRYAKALVEALGEDRLASTLEWLKGSESAFGTEAFQEMLASPQISKTLKGQVVLDVLGDGEAKLLNFIKVLADKNRLELIPDVCKELEKSIAATRNEYVAVLTTQEAFDDKTLKAIEETLAKKLQAKLVLSQKREEFEGVKLVVEDLGVEVSFSRERFINDLKNHILKAF | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q5GSX0 | MKRTQYNNLVSSYARALFLVSENKLSVVRKEVEFLLAFFKSQHDVFIYLSHPMISFARKKEVIFSVNEHLSESLVKFIAVIFANKRSNLLISVLEKFLTLVRESENELEITIKSAETLSESNIKIITESLSFLGKIVRVDNAVDPSILGGFIVKYGFNLIDASLKSYLDRLVDLSKVEILKTRNFI | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
C0R2Y3 | MKKTQYNNLVSSYARVLFHVSGSRLGIIREEVEFLLAFFKDQRDVFVYLSHPMISFAHKKEVMLSINEHLSENLVKFIMVIFANKRSSLLILILEKFLSLARENENEFEITIKSAETLKESDIKIITESLSFLGKIIKVSNVVDPSILGGFVVRYGFNLIDASLKSYLDRLVDLSKMEILKVRNFV | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q8PGG4 | MSQALTLARPYGRAAFAIAREGGNFAPWSDALAFSAQVAGDPRVAALLLNPALGQEQAVTLLAPPQAGEDYLRFLGVLADAQRLSLLPEVAGLYEHLRAEAEHVVKATVTSAAAMSQTELDTIAAALKKRFGRDVDITTAVDASLIGGAVIDTGDVVIDGSLKGKLARLQSSLAH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q3BP12 | MSQALTLARPYGRAAFAIAREGGNFAPWSDALAFSAQVAGDPRVAALLLNPALGQEQAVTLLAPPQAGEDYLRFLGVLADAQRLSLLPEVAGLYEQLRAEAEHVVKATVTSAAAMSQTELDTIAAALKKRFGRDVDITTAVDASLIGGAVIDTGDVVIDGSLKGKLARLQSSLAH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q4UQF1 | MSQALTLARPYARAAFAIAREGGKFAPWSDALAFSAQVAGDPRVAALLLNPALHQDQAVTLLAPPAAEADYQRFLGLLADAQRLALLPEIAGLYEQLRAEAEHVVKATVTSATDMSPAELATITAALKKRFGREVDVTTAVDASLIGGAVIDTGEMVIDGSLKGKLARLQNSLAH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B0RWC5 | MSQALTLARPYARAAFAIAREGGKFAPWSDALAFSAQVAGDPRVAALLLNPALHQDQAVTLLAPPAAEADYQRFLGLLADAQRLALLPEIAGLYEQLRAEAEHVVKATVTSATDMSPAELATITAALKKRFGREVDVTTAVDASLIGGAVIDTGEMVIDGSLKGKLARLQNSLAH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q8PCZ8 | MSQALTLARPYARAAFAIAREGGKFAPWSDALAFSAQVAGDPRVAALLLNPALHQDQAVTLLAPPAAEADYQRFLGLLADAQRLALLPEIAGLYEQLRAEAEHVVKATVTSATDMSPAELATITAALKKRFGREVDVTTAVDASLIGGAVIDTGEMVIDGSLKGKLARLQNSLAH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q2P7Q7 | MSQALTLARPYGRAAFAIAREGGTFAPWSDALAFSAQVAGDPRVAALLLNPALGQEQAVTLLAPPQAGEDYLRFLGVLADAQRLSLLPEVAGLYEHLRAEAEHVVKATVTSAAAMSQTELDTIAAALKKRFGRDVDITTAVDASLIGGAVIDTGDVVIDGSLKGKLARLQSSLAH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B2SQB3 | MSQALTLARPYGRAAFAIAREGGTFAPWSDALAFSAQVAGDPRVAALLLNPALGQEQAVTLLAPPQAGEDYLCFLGVLADAQRLSLLPEVAGLYEHLRAEAEHVVKATVTSAAAMSQTELDTIAAALKKRFGRDVDITTAVDASLIGGAVIDTGDVVIDGSLKGKLARLQSSLAH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q5H4Y7 | MSQALTLARPYGRAAFAIAREGGTFAPWSDALAFSAQVAGDPRVAALLLNPALGQEQAVTLLAPPQAGEDYLRFLGVLADAQRLSLLPEVAGLYEHLRAEAEHVVKATVTSAAAMSQTELDTIAAALKKRFGRDVDITTAVDASLIGGAVIDTGDVVIDGSLKGKLARLQSSLAH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
A7IH28 | MAAQGARHGLQVRERCGVADTIVSGMAGRYATALFELATEAGAVDSVKADLDRLSALIAESADLARLVKSPVFSAEEQLKAISAVLDQAGISGLAGNFVRRVAQNRRLFALPRMVADYASLVAAMRGETTAQVTVPAPLSDAHFFALKDALAQQTGKDVILDVTVDPSILGGLIVKLGSRMVDASLKTKLNSIRHAMKEVR | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B2I863 | MIQALTLARPYARAAFAIACEKGKCMQWSQALTFSAQVANNPIVATLLSHPQLDHEQAAALLSPEGADPAYIRFLEVIAEAHRLDVLLQVAGLYEKLRAEAQHVIKAKITSAIELAPNELNNIVTALKKRFDCEIEVTTGVDHSLIGGAVIDTGNVVIDGSIKSKLTRLQASLTH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q9PE82 | MSQALTLARPYARAAFAIACEKGKCMQWSQALTFSAQVANNPIAAALLCHPQIDHEQAAALLSPEGADPAYVRFLEVIAEAHRLDVLLQVAGLYEKLRAEAEHVIKAKITSAIELAPNELNNIVTALKKRFDCEIEVTTGVDHSLIGGAVIDTGNVVIDGSIKSKLTRLQASLTH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B0U5A1 | MSQALTLARPYARAAFAIACEKGKCMQWSQALTFSAQVANNPIAATLLSHPQLDHEQAAALLSPEGADPAYVRFLEVIAEAHRLDVLLQVAGLYEKLRAEAEHVIKAKITSAIELAPNELNNIVTALKKRFDCEIEVTTGVDHSLIGGAVIDTGNVVIDGSIKSKLTRLQASLTH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
Q87E87 | MIQALTLARPYARAAFAIACEKGKCMQWSQALTFSAQVANNPIVATLLSHPQLDHEQAAALLSPEGADPAYIRFLEVIAEAHRLDVLLQVAGLYEKLRAEAQHVIKAKITSAIELAPNELNNIVTALKKRFDCEIEVTTGVDHSLIGGAVIDTGNVVIDGSIKSKLTRLQASLTH | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(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 delta chain family. |
B8HP54 | MTLTVRVIAPDKTVWDSPAEEVILPSTTGQLGILSGHAPLLTALETGVMRVRSGKEWLPIALMGGFAEVENNEVTILVNAAERGDRIDRAQAEASYAAAQTKLSQAEQSDSRQAKIQAVQELKRARARVQAAGGVVEI | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
P48083 | MSLDVRVIAPNKVIWAKNAEEVILPSQSGMLGILTSHAPLYTALNTGVMKIRNETGWTSIVVMGGFVEVEKNEVLVLVNAGEYVDEIDLSAAKKDVEKALETFNSAEAPKEKEEAAEFLKYAQARLKAVVDK | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
Q0G9V6 | MTLNLCVLTPNRTVWNSKVNEIILSTNSGQIGVLPNHASVATAVDIGILKIRLDGQWLTMALMGGFAIIGNNEITVLVNDAEKGSDIDSQEAQQTLEIAEANFRKAEGKRQKIEANLALRRARTRVETINAIS | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
Q477Z0 | MAMTVHCDVVSAEESIFSGLVEIAVFPGEAGELGILPRHTPLLTRIKPGTIRLKVPDQSEFELVYVSGGMLEVQPDMITVLADTAIRAHDLDEAKALEAKKRAEEALANRNAEMDYAAAEAELAQAVAQLQAIQRLRKHTH | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
Q3Z8Z1 | MAKLKLDIVTAERSVFSEEVDLVVAPGIEGEMAILPHHAPLMTALQAGELKAKIGSEEYSMVVSGGFLEVRPDRVIVLADSAERAEEIDIARATEAKKRAEARMADKYEPGMLAAETEASLRRAMIRLKVAEKRRKRPSV | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
A5FRQ6 | MAKLKLDIVTAERSVFSEEVDVVVAPGIEGEMAILPHHAPLMTALQAGELKAKIGTEEYSLVVSGGFLEVRPDRVVVLADSAERAEEIDIARAIEAKKRAEASMADKYVPGMLAAETEASLRRAMVRLKVAEKRRKHPQV | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
Q3ZZT6 | MAKLKLDIVTAERSVFSEEVDVVVAPGIEGEMAILPHHAPLMTALQAGELKAKIGTEEYSLVVSGGFLEVRPDRVVVLADSAERAEEIDIARAIEAKKRAEASMADKYVPGMLAAETEASLRRAMVRLKVAEKRRKHPQV | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
A9BPU8 | MNTIHVDVVSAEESIFSGEARFVALPGESGELGIFPRHTPLITRIKPGSVRIEMADGSEEFVFVAGGILEVQPNCVTVLSDTAIRGADLDAEKAEKAKLEAEEALKNAKSEVDLARAQSELAVMAAQIAALRKFRQKR | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
C0Q977 | MAENIFLEVVTPGASVVSEEAQIVMAPGSEGEFGVLRGHTTFLTSLKIGSLRYKDAAGKERVLFVNGGFAEVLPTKVTVLAESAERRSQIEVERVRAAKARAEKRISERSVGIDILRAEAALRRAIQRLSVIETR | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
B8FGT3 | MAGNILLEVVTPEKIVVSETVQTVTAPGSEGEFGVLVGHTPFLATLKLGTLNFKDETGKVRAVFINGGFAETLPNKVTVLAESAERRCDIDADRCRLALERAQQRLESKENAVDFERAKRALARAQTRMSLAESRKMDGFQ | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
B1I6J6 | MAEATQKVSIVTPERVIYGDEARFVHVRGTDGDLGFLPGHTPLISSLRPGLLRIQKEGQWSTFVVAGGFVEVRDSRVVVLANAAERPEEIDLARAEKAKERAEKRLAAKDPEIDVVRAKAALARAVARIEAAGQIKR | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
B8FZ33 | MAGTFTLRVVSPEGNVLKEEAEFVVLPGGNGEIGILPNHAPLISSIEIGVIRYTVNGKVEKIATSGGFVEVSDNKVTILADTAEPGERVDLDRALAAKERAEKRLTQREGIDVRRAELALMRAVARINAARN | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
Q24MP2 | MAGTFTLRVVSPEGNVLKEEAEFVVLPGGNGEIGILPNHAPLISSIEIGVIRYTVNGKVEKIATSGGFVEVSDNKVTILADTAEPGEKVDLDRALAAKERAEKRLTQREGIDVRRAELALMRAVARINAARN | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
A8ZUA2 | MAENLRLEVVTPEKTVVSDDAQIVMAPGVLGEFGVLVNHTPFLTSLMPGALHYKDTGEKEHLLFVSDGFAEVLPDRITVLVESAERKEDIDLQRAEAARERAEKRLESGEDVDFVRAKAALTRAIQRIRVAGA | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
Q6AQ09 | MAQQINLEVVTPSGSIINKDVDIVNAPGSGGDFGVLANHAPLLSTIKIGALTYEIGEERNTLMVSGGFCEVSNNKITFLVESAEAKQDIDTDRAMKAKIRAEKRIAKHGLPSDEAYSDTRAEAALHRALIRLRVAQGL | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
A4J998 | MAKTQRLDIVTPEKVVFSEEIDFVVAPGADGELGILPEHAPLVTALKVGTLRVQQGGKFFKVAVSGGFMEVKNSRIVVLADTAERADQIDVERAKAAKQRAEQRLNSKGSEIDVHRAEIALHKAINRIKAAE | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
Q72E05 | MEKSLHLEIVTPDKLVLSEQVDYVGAPGFEGEFGVLPSHIPFLSALAIGSLYYKANGKTHHVFVSGGFAEVSDNKVTVLAESAERAEDIDIDRARKAKDRAEQRLAQIKEKVDHARAQAALQRALARMRVRGNA | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
B8DRD3 | MEKSLHLEIVTPDRLVLSEKVDYVGAPGYEGEFGILPNHIPFLSALNIGSLYYKAGGKTHWIFVSGGFAEVSDNKVTVLAESAERAEDIDLERARKAKERAEQRLAQAKEKLDSARAQAALQRAMARMRVRGAA | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
A1VFJ6 | MEKSLHLEIVTPDKLVLSEQVDYVGAPGFEGEFGVLPSHIPFLSALAIGSLYYKANGKTHHVFVSGGFAEVSDNKVTVLAESAERAEDIDIDRARKAKDRAEQRLAQIKEKVDHARAQAALQRALARMRVRGNA | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
P30159 | MSINIRIVTPTGFLWETKAEEILLPSTTAPLIVLPGHINILTGLSPGLLRVKVDSRWKPILISSGAAQILTSDSTNVDVGIMEVEEIKQENFKEAELLLEKANDALNIINPIDIRERIKAGEAKSFAESRVEAFKFLAT | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
Q9TKI6 | MTLNLCVLTPNRTVWDSEVKEIILSTNSGQIGVLKNHAPIATALDIGILKIRLTNQQWVTMALMGGFARIGNNEITILVNDAEKSIDIDPQEAQQTLKIAEANLNKAEGKRQTIEANLALRRARTRVETILESINRF | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
Q9MUT4 | MSFQVRIIAPNGIIWDSEAEEIILSTNTGKIGVLTNHTSLLTGLDIGTIRIRALNNQWNTLALMSGFAVIKDNVATIIVSEAENGANIKSEEAQTQLEEAKSYFNTAKGTKNEVEANLAVKRAETRLKASQNL | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
Q1GXN1 | MASTIHLDVVSAEESIFSGEAEFVAAPAKLGEVGIYPNHAPLITTIKPGVLRVKVANGGEEQAIYISGGLLEVQPGVITVLADTAIRGHDLDEVKAIEAKRAAEEALRNNASGVDYARAQAELSEALAQLQTIEQLRKTTH | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
A2SC71 | MATIHVDVVSAEASIFSGEAKFVALPGEMGELGIYPRHTPLITRIKPGAVRVERADNGEEEFVFVAGGILEVQPDRVTVLADTAIRGHDLDEAKAEEAKKAAEEAMKNAKSDIDFAKAQGEFAAMAAQIAALRKFRKK | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
B8EQQ2 | MPDFHFELVSPERLVFAGAVESVVVPGTEGQFTVLKDHAPLMTTLKPGVIDIAESKALLHRFFVRGGFAEVSPAGLTILAEQAIPLESLDAARIDADIKDAEEDIADASVDETRRLAAEKRDQLLELKAALKI | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
B0JFM8 | MSITVRVITPDRIVWDNVAEEVILPSSTGQLGILSGHAPLLTALNIGVMRIRPGKDWENIAVLGGFAEVENNEIKVLVNGAELGSKIDKEKARAEYERAQTRLDEVSKGDDRRKTIQAQQSWRKARARYQAAGGLVSV | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
C5CA79 | MAELNVEIVSEERSIWSGAASAVSARTVNGEIGILPGHTPMLAVLGDGEVVVRTTDGGTVTAQAHGGFFSVDHDRVVIAATSARLGDAAAA | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
Q2RFY0 | MASLNLEIITPERVVLQAEAASVIAPGIQGYLGVLPEHAPLITPLQAGVVTCRRRERAEERVAVSGGFLEAGPDQVIILADTAERSEEIDVEWARQARERAERRLRERPPGLDVARAEAALRRAVARLKAAGAI | Produces ATP from ADP in the presence of a proton gradient 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 (By similarity). In this bacterium the a and b subunits are transcribed but do not seem to be translated, thus the ATP synthase consists of the alpha, beta, gamma, delta, epsilon and c subunits. Belongs to the ATPase epsilon chain family. |
Q09X11 | MTLNLCVLTPNRIVWDSEVKEIILSTNSGQIGILPNHAPIATAVDIGILRIRLNDQWLTMALMGGFARIGNNEITVLVNDAEKGSDIDPQEAQQTLEMAEANLSKAEGKRQTIEANLALRRARTRVEAINMMS | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
A0QCX9 | MAELNVEIVAVDRKIWSGEATFLFTRTTVGEIGILPRHIPLVAQLVDDAMVRVEREGEDDLRIAVDGGFLSVTEETVTILAESAEFSSEIDESAAREAAESDDPRVAARGRARLRAVGAID | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
B1MLW3 | MSEIDVEIVAVEREIWSGKATFVFTRTTSGEIGILPHHIPLVAQLVDDAAVKIEREGSDDLWWAIDGGFLSITDTKVSILAESAQARADIDEAKAKTDSGSEDPRVAAQGRARLRALGQTV | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
X2BHY8 | MAELNVEIVAVDRNIWSGTAKFLFTRTTVGEIGILPRHIPLVAQLVDDAMVRVEREGEKDLRIAVDGGFLSVTEEGVSILAESAEFESEIDEAAAKQDSESDDPRIAARGRARLRAVGAID | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
A1KI99 | MAELNVEIVAVDRNIWSGTAKFLFTRTTVGEIGILPRHIPLVAQLVDDAMVRVEREGEKDLRIAVDGGFLSVTEEGVSILAESAEFESEIDEAAAKQDSESDDPRIAARGRARLRAVGAID | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
C1AMV5 | MAELNVEIVAVDRNIWSGTAKFLFTRTTVGEIGILPRHIPLVAQLVDDAMVRVEREGEKDLRIAVDGGFLSVTEEGVSILAESAEFESEIDEAAAKQDSESDDPRIAARGRARLRAVGAID | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
P33255 | MVKLKVLSPNGTLFDEKIEMVIVKGAEGYAGFMRNTQPSIFAINNSVGYITYPDKTKKSVVIENATLYCNKDLIKIFALDFVIADNLSYDEIMKRKKDLESKIKDTTDTKELIRLQHALDIELLKLKEAK | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
P47638 | MKLLRFLVLSPSGIKLDKTIISAQVKTTEGYIGLNFNRAPLIAAIQSHLCKIIFADQTKREAIIGAGLMLIKKTEAKIFTENFVFADEVDINETLKRKTELERKIHHIKDAKLNVKIEQNLMFELLKLSSKKK | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
A4T8K3 | MADLHVEIVAVERELWSGDATFVFTRTTAGEIGILPRHIPLVAQLVDDAMVRVEREGEDDLRIAVDGGFLSVTEEAVRILVENAEFESEINADAAKQDSESDDERTAAWGRARLRALGQLD | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
B8ZR43 | MDELNIEIVAVDRKIWSGKGTFLFTRTTAGEIGILPRHIPMVAQLVDDNMVRIEREGEKDLRVAVDGGFLSVTEERVSILAESAEFDSEIDENAAKQDAESDDPRIAARGRARLRAVGAID | Produces ATP from ADP in the presence of a proton gradient 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 epsilon chain family. |
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