ids
stringlengths 6
10
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stringlengths 11
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stringlengths 108
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Q8KGE7 | MRKKAISRILALVVPVLLSLNSQAFATSVQDESPVTGSAVEAVHTVPSTVAAPVAGHAEAAAGQAAKAEEKPGDLIMHHILDNSTFSFEPFGEVHLPHLEVAGFDISITKHVVMIWLAAILLVVIASAAGASVKKMSANQAPKGVANVFESLVDFISNDVAKPNIGHGYEKFLPYLLTVFFFILVCNLLGLIPYGATATGNINVTLTLSVFTFVITQFSAFKAQGVKGYLQHLTAGTHWALWIIMVPIEILGQFTKPFALTIRLFANMTAGHIIILSLFFISFILKSYIVAVAVSIPFAIFIYLLELFVAFLQAYVFTMLSALFIGLATAHSDSHDGHELEATARHGDGLTV | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37818
Sequence Length: 352
Subcellular Location: Cell inner membrane
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Q2S6N5 | MAGENPTASEYIQHHLQNLTFGNHPEHGWSFAHTAQEAKEMGFWAVHVDSLGWSIALGALFVWLFRKAAVKATSGVPSGLQNFVEIMVDFVDKSVKETFHGKNAVIAPLALTVFCWIFLMNLMDLVPVDFLPRLFQVITGDDHAYFKVVPTTDVNVTLGMSLSVFFLIIYYSIKVKGVGGFLGELTLQPFGKWMLPFNLLLEGVGLIAKPISLALRLFGNLYAGELLFILIALMPFWAQWALSVPWAIFHILVIVLQAFIFMMLTIVYLSMAHEDH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30919
Sequence Length: 276
Subcellular Location: Cell inner membrane
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A9IQH9 | MTAHAPDPIHQFEVSRLIKISIGNMDLSFTNVSLFTVVTVVITAAFLFISSSSRGLVPTRMQSLSEMAYEFVASTLRESSGVQGMQFFPLVFSLFTFILVANFIGLFPYFYTVTSQIMITFSLAMVVILTVIGYGFYKHGISFLKLFVPSGVPVVVLPLVTMIEIISFLSRPISLSLRLFANMLAGHITLKVFAGFIVSMIGVGIVGVGGAVLPLIMTVAITALEFLVAFLQAYVFTVLTCMYLNDAIHPGH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27502
Sequence Length: 252
Subcellular Location: Cell inner membrane
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Q6MRR3 | MSFNWTQLVPGVGHEYAHVATLGIATVAAVGIGAAARASLGKGEAAVLPASKFSLRGIFELLTEMTSGLADMVIGEHGKHYIPFFASVFFFILFNNLLGMIPGMTPATENMNTTFGFGVLMFLFYNFQGVKENGPVAYLKHFMGPVIFLAPLMFVIEIVSHIVRPFSLGLRLANVMMGDHTVLSVFLDLVPIGVPIPFYVMGLFVCFVQAFVFTLLSMVYVAFAIAHDH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24920
Sequence Length: 229
Subcellular Location: Cell inner membrane
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Q2KU30 | MAAASGASPQSEYIQHHLVHLNNLGEKQSVIAQFNVINYDSLFWSGLMGLIVIFCLWLAARRATAGVPGRFQGFVEMIVDMVNDQAKGIVQNAKSREFVAPLALTVFLWIILMNALDLLPVDLFPTIWRVTGLGAEHGDPLYYHRILPTADLNVPMGMSLGVLLLMFYYGIKIKHPAGFVKELFTAPFHAHGLAALVLAPFNLLLNLIEYAAKSVSLGMRLFGNMFAGELIFMLIALLGGAWTGFNASSIGLGIGHVLAGSVWAIFHILIVLLQAFIFMMLTLVYIGQAHEGH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32076
Sequence Length: 293
Subcellular Location: Cell inner membrane
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P00847 | MNENLFTSFITPVILGLPLVTLIVLFPSLLFPTSNRLVSNRFVTLQQWMLQLVSKQMMSIHNSKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMSISTTTALITFTILILLTILEFAVAMIQAYVFTLLVSLYLHDNT | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24788
Sequence Length: 226
Subcellular Location: Mitochondrion inner membrane
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Q34946 | MMPDIFSSFDPYMFNTLFPLNSLFLVTNTAIILMIQSSFWVLNARTSAFKSPVNDTIFTQLSRTSTTHLKGLSTPLSTIFFMLVMINLMGLIPYMFSTSSHLVFTLSLGFPIWLSLMISTFAHSPKKSTAHFLPDGAPDWLNPFLVLIETTSVFVRPLTLSFRLAANMSAGHIVLSLMGIYCAAAWFSSVSSTALLILTAIGYILFEVAICLIQAYIFCLLLSLYSDDHAH | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25678
Sequence Length: 231
Subcellular Location: Mitochondrion inner membrane
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A0LDW6 | MSAEAMHAAASAAPKMDPLHHFMVQKVVPIEIAGIDLSITNSTIWMWLAVAVAFLFMKWSFRGRAEDKLIPTKMQSLAEMTFTFVRQIVDQNIGGAEGRKYFPAIFTLFLLVLFCNLLGLIPGSFTPTSQLVVTATLALSVFFFATGLAIVKHGTGFIGFFVPSGVPPMLLILMVPIEIVSYLSRPVSLSVRLFANMTAGHTVLAIMFFFAATLPLGGLLMPAAFATVFTGFELFIGFIQAYIFTILTCVYINDALHLH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28338
Sequence Length: 259
Subcellular Location: Cell inner membrane
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Q2W028 | MANPIEQFKIQPLVPLKVGSVDISFTNSSAMMVLSICLITLFLTLSVRSRALVPGRWQSMAEVFYEFIAGMLRDNVGQEGRKYFPFIFSLFMFVLFGNLLGMMPIPVIGFTYTSHVIVTFAMALVVFVGVTVIGFARHGTHYLRMFFPHGAPIATAVILIPIELISYFSRPFSLAVRLFANMTVGHIILKVMGGFVVSLGAFYLIPGAVPFAFLSAITVLEFGIALLQAYVFTILSCIYLHDAIHMH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27374
Sequence Length: 247
Subcellular Location: Cell inner membrane
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P26853 | MACSPLEQFAIIQLIPIHIGNLYFSFTNSSLFMLLTISLVLLLVHFVTLNGGNLVPNAWQSFVEMIYDFVLNLVNEQISGASSVKQRFFPLIYVTFTFLLFCNLIGMIPYSFTVTSHFIITLGLSFSLFIGITIVGFQTHGLHFFSILLPQGVPLPLAPFLVLLELISYCFRALSLGIRLFANMMAGHSLVKILSGFAWTMLSMGGILYLGQLAPFFIVFALTGLELGVAILQAYVFTILLCIYLNDAINLH | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28009
Sequence Length: 252
Subcellular Location: Mitochondrion inner membrane
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O47494 | MGAAYFDQFKVVDLIAITNSSMMMMLAVAVALILLKGNRLIPNRWQAVMESIYDHFHGLVKDNSGPQYFPFVFTLFIFIVFLNILGLFPYVFTVTVHIVVTLGLSFSIVIGVTLGGLWKFKWNFLSILMPAGAPLALAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLTTAGVFNIFPVLIMVFISLLEAAVAVIQAYVFSLLTTIYLADTIVLH | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25098
Sequence Length: 229
Subcellular Location: Mitochondrion inner membrane
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Q2RFX3 | MTHVRPVEIFHLGPIPIYSTVVNTWIIMILLLAGIFLATRKLSFIPRGAQHVLEMFLEFFYGLLEEIIGKEGRRYLPLVATLFIFILSLNLSWFIPGMKPPTMDLSTTAAFAVTTIILVQIFGIRKLGLRGYIRHFFQPAPFLFPLNVIEELVKPVSLSLRLFGNLFGEEMVVTILFLMIPFLLPTPIMLLGVLMGTIQAFVFTLLTITYIANFVHGH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24723
Sequence Length: 218
Subcellular Location: Cell membrane
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P00848 | MNENLFASFITPTMMGFPIVVAIIMFPSILFPSSKRLINNRLHSFQHWLVKLIIKQMMLIHTPKGRTWTLMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVITGFRHKLKSSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLLLTILEFAVALIQAYVFTLLVSLYLHDNT | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25096
Sequence Length: 226
Subcellular Location: Mitochondrion inner membrane
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P80497 | MRQFDPWPVFFRREWSRNWPFLVGFAVTGAIITKMSLGFTEEERKNSRFAQRHKN | Function: 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 (Probable). 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 (Probable). 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 (Probable). Part of the complex F(0) domain (Probable). Confers tolerance to several abiotic stresses (e.g. salt, mannitol, drought, oxidative and cold stresses), probably by providing additional energy needed for cell homeostasis (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6705
Sequence Length: 55
Subcellular Location: Mitochondrion inner membrane
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Q02B01 | MFNDHLAGAGNALTGIVGMAPEARPWANFVTMQLLVVAIIVVLFAILRPRLSPDRPGKLQHTFELVYGFLHEQAEEQIGHEGHHYLAFFGTIFIFILFANLIGVVPGFEAPTMVPSVPAGCAIAAFFYYNIVGVQANGLGRYLAHFAGPMPLLAPLMIPIELVSHMARPLSLTIRLFANMYAGEQVTMVFLKLTFLFVPAVFMGLHVFVSFLQAYIFMLLTMMYVAGAVAHEH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25668
Sequence Length: 233
Subcellular Location: Cell inner membrane
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A9FGS5 | MPEHTGFLTYLLAQLPGLRENARNIGKTFIGHHTVDYRGTEPIFMSLLIMVLFVLLASEVRGQYRRLNESVIPEDKLTLRTFFEAFFGYFYGMARDVMGPANAKRYFPLIGGSAAFIFFSNASALIPGVNPPTSNLNITIGCAVVVFVLFNYYGLKENGWSYVAHLAGPKWYLAPLIFPIEVISTCVRPVTLSIRLMLNIGVDHLVASIFLGLVALFVPVPLMFLAIIVIVVQTLVFCLLSCIYIGLATEKADHH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28338
Sequence Length: 255
Subcellular Location: Cell inner membrane
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P80086 | SPLEQFSILMLIPM | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 1619
Sequence Length: 14
Subcellular Location: Mitochondrion inner membrane
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Q9TBI7 | MPQLNPNPWLFIMLMSWLTFSLIIQPKLLPFTPINPPSNKTPTTTKTSPWTWPWT | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6453
Sequence Length: 55
Subcellular Location: Mitochondrion membrane
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A9RAH3 | MPQLVPFYFTNLLTFGMLAISMLLYLVSTIILPNILRLLVARTTMTKL | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5487
Sequence Length: 48
Subcellular Location: Mitochondrion membrane
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Q36362 | MPQLLPTPWFTIFIYAWMVLLAVIPLKILSYVYPNHNYLRGLQKPSEHSWFWPWS | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6691
Sequence Length: 55
Subcellular Location: Mitochondrion membrane
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P84345 | MPQMAPISWLLLFIIFSITFILFCSINYYSYMPNSPKSNELKNINLNSMNWKW | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6365
Sequence Length: 53
Subcellular Location: Mitochondrion membrane
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Q7UH05 | MTTYSETLETAAQQFDQAVKSQPSQLTVTEIGTVEEVQRGIARVHGLPHVQVDEVLRFAGGHLGYAFNLDPDQVGCVLLDSSDQITAGSRVERMHSVLDTPVGDQLLGRVVDPVGRPLDGGRSLDDLPREPCERDAPPIMQRAPVTVPLQSGLKVVDAMIPIGRGQRQLLLGDRQTGKTAIAIDTIINQLGRDVICIYCSIGQRSTGVARVIENLRRHDALDHTIVVIGADDAPPGLQFLAPYAATTMGEHFMRQGRDVMIVYDDLTSHARAYRHLSLLLRRPPGREAFPGDIFYVHSRLLERSTHLIQSAGGGSLTALPIIETEAQNVSAYIPTNLISITDGQIYLSPTLFRKGVLPAIDVGRSVSRVGGKTQLPAYRVVAGDLRLTYSQFEELERFARFSSQLDEDTRATLDRGRLIREILKQTQFQPLTLPQQIASLIAVTNGVLDGVPVDQLPTIERAIQDAVTSQANDLCAQMQSGKKLDKQQVGQIANIAAGAVHAHA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54920
Sequence Length: 504
Subcellular Location: Cell inner membrane
EC: 7.1.2.2
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B8D8H1 | MRLNSTEISKLIKERIAQFEVFNQSYNEGSIISVSDGIIKINGLSNVMLGEMILLPNNEYAIALNIERDTVGAVVMGPYIHISEGAKVRCTGKILEVPVGDNFLGRVVNALGFPIDGKDSIQNDGFFPVEADAPGVIDRKSVNQPIQTGYKVIDSMIPIGRGQRELIIGDRQTGKTALAIDTIINQKQSGIKCIYVAIGQKLSTIINVVKKLEENNALFNTIIVVASASEAASLQYLAPYSGCAMAEFFRNKGEDSLIIYDDLSKHAVAYRQISLLLRRPPGREAFPGDIFYLHSRLLERASRVSMEYVQKITKNKITGKTGSITALPIIETQSGDVSAFVPTNVISITDGQIFLESNLFNSGIRPAVNPGISVSRVGSAAQTTIIKKLSSGIRTALAQYQELAAFSQFSSDLDDTTRKQLNHGQKITELLKQKQYSPISIAEQALILFVAENNFLDDISIDKITKFEKEILIYAHNYYFDLMEEINKTGDFNIVIKDKFIKLITEFKKNQF | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56636
Sequence Length: 512
Subcellular Location: Cell membrane
EC: 7.1.2.2
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Q89B41 | MQISSSEICELISKKIAKFDIISSMHNEGRVISVSDGIIQIYGLSDVMQGEMLSLPGDKYAIALNLEKNVVGAIVMGEYTHITEGTKIISTGRIFEIPVGSKFLGRVINALGVPIDGKGRIQEEKFLPVEINAPGVIDRQKISEPLQTGYKSIDAMVPIGKGQRELIIGDRQTGKTSLAIDTIINQRNTKIKCIYVAIGQKFSTIVNLVRQLEDNQALNHTIVIVASASESAALQYLVPYSGCSLGEFFRDQGKDALIVYDDLSKHAIAYRQISLLLRRPPGREAFPGDIFYLHARLLERACRVNSNYLKNILGTVNKFSTGSLTALPIIETQDGDVSSFIPTNVISITDGQIFLESNLFNSGIRPAINPGISVSRVGGAAQCQIIRKLSSGIRTSLAQYQELIAFSQFSSELDEITRNQLIHGKKLIEILKQKQYHPMSIAEQAIILFAAENNFLNDVSVEQIIKFEKMLLLFFNTNNSELVLSINNYKRINDVVENQLSDVINAFKLTKCWS | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56888
Sequence Length: 514
Subcellular Location: Cell membrane
EC: 7.1.2.2
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Q9XXK1 | MLSKRIVTALNTAVKVQNAGIATTARGMAGASGSEVSKILEERILGTETGINLEETGKVLSIGDGIARVYGLKNIQAEEMVEFDSGIKGMAMNLDVDNVGVVVFGNDKVIREGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTIINQKRFNDAGDDKKKLFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDASTQQLLNRGVRLTELLKQGQYVPMGIEEQVGVIYAGVKGYLDKVDPSAITKFEKEFLAHLRSSQQALLKTIREEGQISPQTDAQLKDVVVNFLATFKP | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (Probable). Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). Binds the bacterial siderophore enterobactin and is required for the assimilation of enterobactin-bound iron from non-pathogenic bacteria. Promotes mitochondrial accumulation of enterobactin-derived iron ions .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57788
Sequence Length: 538
Subcellular Location: Mitochondrion
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Q4FP36 | MDINPSEVTKILKEQIKKFGDKAEVTEVGQVLSVGDGIARVYGLDNVQAGEMVEFSDGSKGMALNLESENVGVVIFGDDRKIKEGDVVKRTGSIVDTPVGKELLGRVVDGLGNPIDGKGALDKATKRSRVEVKAPGIIPRQSVSEPMQTGLKSIDSLVPVGRGQRELIIGDRQTGKTAVAIDAIINQKKINESGDEKQKLYCIYVAIGQKRSTVRQIQKTLEEAGAMEYTTIVAATASDAAPLQFLAPYTGCTMGEYYRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEHGGGSLTALPIIETQGGDVSAFIPTNVISITDGQIFLETELFNQGIRPAINVGLSVSRVGSAAQTKAMKKVSGSMKLELAQYREMAAFAQFGSDLDASTQKLLNRGSKLTELLKQKQYSPMTVAEQVISVFCGVKGYLDDVELKDIAEFESKIIEKCKSEKPEILESVLSSGKLEEDTEKSLVDTIMELKKNFNS | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55569
Sequence Length: 511
Subcellular Location: Cell inner membrane
EC: 7.1.2.2
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P06541 | MSDSIETKNMGRIVQIIGPVLDIVFAKGQVPNIYNALTIRAKNSAGTEMAVTCEVQQLLGDNCVRAVSMNPTEGLMRGMEVVDTGKPLSVPVGKVTLGRIFNVLGEPVDNMGNVKVEETLPIHRTAPAFVDLDTRLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFAGVGERTREGNDLYTEMKESGVIVEKNLSDSKVALVYGQMNEPPGARMRVALTALTMAEYFRDVNKQDVLFFIDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQPWILGEKHYDSAQSVKKTLQRYKELQDIIAILGLDELSEEDRLIVARARKIERFLSQPFFVAEVFTGSPGKYVSLAETIEGFGKIFAGELDDLPEQAFYLVGNITEAISKAASLK | Function: 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.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 52040
Sequence Length: 481
Subcellular Location: Plastid
EC: 7.1.2.2
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Q09MH1 | MRINPTTSGPGVSAFANKNLGHIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTVDQPINVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGAPLSVPVGGVTLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLDTRLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINDQNLSESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELDGLPEQAFYLVGNIDEVTAKATNLEMESNLKK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53636
Sequence Length: 498
Subcellular Location: Plastid
EC: 7.1.2.2
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Q0C100 | MSTPANGKGRISQVIGAVVDVEFDGELPSILNALETFNNGSRLVLEVAQHLGENTVRTIAMDSTEGLVRGQPVSDIGTPITVPVGPATLGRIMNVIGEPIDERGPVNADTYMPIHAQAPAFVDQATESEVLVTGIKVIDLLCPYAKGGKIGLFGGAGVGKTVLIMELVNNIAKLFGGYSVFAGVGERTREGNDLYHEMIESNVINLEGESRMSLVYGQMNEPPGARARVALTGLTQAEYFRDVEGKDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPATSFAHLDATTVLNRAISEKGIYPAVDPLDSTSRILDPMVVGEEHYEVARGVQQILQKYKELQDIIAILGMDELSEDDKVTVARARKVERFLSQPFDVAQVFTGSPGVQVKLEDTIKGFKGLISGEFDHLPEPAFYMVGNIEEAKAKAAKLMADAA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50900
Sequence Length: 475
Subcellular Location: Cell inner membrane
EC: 7.1.2.2
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A8Z6C7 | MINKVKGKIIQIIGPVIDVLFENVSSLPMIYDSLEVFNPKGNQIILEVQQHIGECTVRCISMDITDGLKRGQDVFSLGTTISMPIGEEINGRVFNVVGNTIDGLGDLNNSKRISIHRNPPKFEYLSTNIDILYTGIKVIDLVEPYIKGGKIGLFGGAGVGKTVLIQELINNIAKGYGGLSVFAGVGERTREGNDLLREMISSGIIKYGDSFLEDMKNGKWDISKVDKNELKNSKATFVFGQMNEPPGARARVVLSGLTLAEYYRDSFRKGRDVLFFIDNIFRFTQAGSELSALLGRMPSAVGYQPTLASEMGTMQERITSTKNGSITSIQAVYIPADDLSDPAPATTFSHLDATTVLSRKISSLGIYPAVDPLSSTSRILSIEFIGNDHYLCAQRVKQILQRYQELQDIIAILGIEELSEEDKIIVHRARRVQRFLSQPFNVAEQFTGITGKLVNIKDTIEGFNLILDGKLDNIAEVHFNLKGTISEVIDSSKKKI | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54690
Sequence Length: 496
Subcellular Location: Cell membrane
EC: 7.1.2.2
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Q07233 | VLIMELINNVAKAHGGYTVFAGVGERTREGNDLYHEMIESGVISLKDKTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTSKGSITSVQAIYVPADDLTDPA | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Sequence Mass (Da): 17042
Sequence Length: 158
Subcellular Location: Mitochondrion
EC: 7.1.2.2
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Q6CFT7 | MVLPRLIPRLSRSAFKVAQANNRVFNAPFRGMASSAGVGSGKIRTVIGAVVDVQFEQDNLPAILNALTIDRGEGNKLVLEVAQHLGENTVRTIAMDGTEGLVRGTSVADTGAPITIPVGRGTLGRIINVCGEPIDERGPIEATKFLPIHADPPTFAEQSTTAEVLETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFCGVGERTREGNDLYREMKETGVINLEGESKVTLVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGALQERITTTQKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDIDVVGQEHYDVASNVQQTLQAYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFTVAEVFTGIEGRLVSLKDTVRSFKEILDGKHDALPEAAFYMVGGIEEVVAKAEKLAAESK | Function: 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 ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk . During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation . Subunits alpha/ATP1 and beta/ATP2 form the catalytic core in F(1) . Rotation of the central stalk against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta/ATP2 subunits .
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54535
Sequence Length: 509
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.2.2
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P00830 | MVLPRLYTATSRAAFKAAKQSAPLLSTSWKRCMASAAQSTPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Sequence Mass (Da): 54794
Sequence Length: 511
Subcellular Location: Mitochondrion
EC: 7.1.2.2
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Q6A8C4 | MTTAVGASQQLDEVGDRRGTGTEFANEIFAVVDVLNRESGLRRAVSDTGSETKARQGLIDAVFTSKVSPDCKELLDATTTCKWRSPAALTRALERQGVRAVLRGARQADRFEAVADELFHVSRLVRGQAALQVALGDPNRSVADRQELLMKLVGGQVSEETLVLARRAVVASDSTFEQVIDGYLHVAAEMADRRRAIVTTAKALTDAQRAEMVKQLERITGSPIELSEVVDPTVLGGALINLGDEVIDSTVAHRLDQARRELG | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28447
Sequence Length: 263
Subcellular Location: Cell membrane
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Q9TM27 | MILLLTNSKIIYPYSEALFSIAKDQEKFEVIKNDMELFVTFTKNLNGFKKFLETPLINKNKKIKVVKDVFSKILNSTTLNFISILINKNRIMFVSNISEKYNQLVLKDKSVKLVKIACARQLSEKQAQALSEVLKHKFKCLSVKLIFNIEPELIAGFKIFIESQVIDVSLQGELKEFEWYLTK | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21232
Sequence Length: 183
Subcellular Location: Plastid
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Q85FQ9 | MKQKIVEPYAQALFRLKDDIDLTPLWEMARDSKFMQLLMNPSIPKEKKWQLFQPFDKLVQSWLEVIWKKKRMNLLAEICASYLELRKKKEGIVTVFVTSATPLTDTQTQQLEVQLTRMCQAKHLQCEYQVDAQLLAGLKIQMNGQLIDTSWQTQLKQLMKSLW | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19233
Sequence Length: 163
Subcellular Location: Plastid
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Q11YP2 | MKETRVAYRYAKSLIDLAAENGVLDRVNADMAGIESVFKQNHQLVAVMKNPIVQGDKKHAILEALFGGKVDNFTMSLLSLLTKKHREAVVFEISSEFQRQYREKMGIKIVEVTTTQPITEDQRANFKAIMASKASKVELIEKIDEKILGGFVLKMDDQQIDESVIAKLNKIKNKFTEQVINY | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20649
Sequence Length: 182
Subcellular Location: Cell inner membrane
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Q477Z4 | MAESVTIARPYAEALFRTAKESGNLAKWSEQVSLLGQVAANPDVSSAIGDPNVAAPQLVDLFRSACGTAVDAELSNFIQLLSNNDRLGLLPEIAGLYETYKRAEEGTKQADIVSAFPIDDNQVKALIPQLEAVFKTKLEAAVSVDPTLIGGIKVIVGDQMLDASVRGKLDAMATALNN | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18858
Sequence Length: 178
Subcellular Location: Cell inner membrane
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Q3Z8Z5 | MAKRVYAIAMRYAQALYELAKEQKSLDKWQEDLQDLSSLTEDASVAEFLSNPKIASARKHKVLAKLSNIDPLMLNLVDMLVATRRLGIMRAVSGEYNRLLNEARGVEDAIVTTAKPSSEADIEIIRQQLSKITGKKINVVTATDPGLIAGLKARIGDKLIDGSVSRRLVLLQNEISQGRI | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19872
Sequence Length: 180
Subcellular Location: Cell membrane
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B1I6L7 | MIKGAVAARYAQALFDVARDNNRIAETENELRGFMRLLDESRDLQQVLYNPQVPVELKKEIVREAFGKELSGTTLNFLCLVLDRRREVYLKGIADHFIALANETRNIIEAEVTSALELSVVHKVNLMQVLSRMTGKELRIRYQVDPDIIGGLVVRLGDRIIDGSIKRQLERLKDSIRETKVG | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20732
Sequence Length: 182
Subcellular Location: Cell membrane
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Q2RFX6 | MSEQNVARRYARALFNIAREQGTAGEFANGLEEVSRTLAENSDFRRVLYHQLIPVREKQKLIDTIFPDINPLLKNFLHLVLAKGRERALPEMAAQFRRLVDQAENILPVEVTSAITLREDILAGLKERLAGITRRNIRLSSRVNPELIGGVVIRLGDRVLDASVKKKLELLGEHLKRA | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20168
Sequence Length: 178
Subcellular Location: Cell membrane
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A5IYE2 | MFIKANADGYALALYDLHKEEKHVSSTYENILSFYELLSNDKEVFSFFNSSKIGLEEKHKIADELVQENKNLKTFANFLKLLISKNNSPLLLQALSIYIRLVESELNILRAKLISAFEIDNQTKIKIIEKLENKYNKKIKLTTFIDKSLIFGFKIVIGNDIIEQNAKADLEKISSLINNKNGDLNG | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21290
Sequence Length: 186
Subcellular Location: Cell membrane
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P33254 | MDTNIMGFARALVDLAHEEDKVHLFYDNLKVVFDLVKENQDLMSLMNSQVLSKNQKHEIIDVVFKDHLTQTIVDFLKVVIDNREFFHIKSIIKKFFRMIEEEEHTIFINVVSAHELNDDQKAQLVEKLHKKFASQVKILYQTDPSLIAGIRIQSNDLLIDNSIDGKLKLLKHQLRTFSKEN | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21175
Sequence Length: 181
Subcellular Location: Cell membrane
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P47642 | MINAQAFGTALFQLSEEQKQVKKIYEECHFFLKLMRNFKDGSLSFLLNSYTLTKPDKIRLVDKLFKNHFCQVFVDFLKVIILKGYFTLVEQAIKYFFDNVESQKHIQFIKIITAFELSSKQLNKIIAIMEKRFKTKVVYKTEIDRSLISGIRIESSSHLFEKNVRDELKRIMAHFI | Function: 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 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20874
Sequence Length: 176
Subcellular Location: Cell membrane
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Q6MS91 | MILKETTINNYATALFNIAVKEKLVDDYIIQVDALIKSLADKDEFNKLVTYSNKEQKKQAILIIENTFSSFGFDIYLINALKILVENQLFINTRMILKVLYKKLLAYKNIVLGEVYSTEKLTKTQLNAIKKKISNKVNKKVELVNKIDPTLIGGIKVSVEDKVFDGSIKAKLEALKKQMNT | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20620
Sequence Length: 181
Subcellular Location: Cell membrane
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Q98QU2 | MIDNHYVQSSAKALSQIAFEEKKEKLFLNQLFIIKNIFSYNPEVVEYLASGSIKLENKKKFIEEIFDLIEPLILNFLLMAVEDNKIKYLDNIFLKAILTINKKLNIENGIIYTTLKLSDKKLLEIEKKLSVFLKKEVKLLNLIDKELISGYEIQVGDFKQRNNVASWIDQMALSIKKGD | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20790
Sequence Length: 179
Subcellular Location: Cell membrane
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Q4A601 | MYVKVNPSSYSVAIYEIAKESNKIKTFHEQFSFVKKVIEKNPQLITFLKNDEIALEKRFELIDEIFGSLEVDVKNSIKVALVRNMIFVLRKIIVDFLKITNYELGIKFAKVITAYPLSDSELEKIQKKLNEKTKKIVEISTEVDEKLLSGYKIIFSNQLYERNYNNDLQKIKKTIIKGKEDEK | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21420
Sequence Length: 183
Subcellular Location: Cell membrane
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Q1CWT4 | MVNVSIARRYARALLDVASEAGRTDAVAEQLTAFADVIAKNAELTDVLVNPAYTREQRLRVVESVMQAIPGGVEATLANTLRLLVDRNRLGYLADIARLFRDMADARAGRVRGHVTSAAPLPADALAQLQQTLQQLTQRNVLLETRVDPSLLGGVSAQVGSILYDGSIRTQLEEMRRELKQR | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19948
Sequence Length: 182
Subcellular Location: Cell inner membrane
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B2A3G5 | MIIPKRYAEALFQLAKEREKINEITQSFNQLIERLRSNEEVFKLLSYPVVDIAEKKQVADELTADLEQEIRDYLKVLIDNKRTDELAEIHDTFLDLVRTEENRTLCEVKTPIPLDEDELKKIQDLLAQMSEGEVEIETTTDESIIGGIVVRIGDRVFDYSLKGQLNSLREQLKKTTITS | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20727
Sequence Length: 179
Subcellular Location: Cell membrane
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B4RJF7 | MAEFATIARPYAKALFGLAQEKNQIESWLGGLEKLAAVVQEGKVALLIDRPETNASEKADILIDLVGLKDKELKNFVIVLAGQKRLSILPEVYAQYQDLTLSFNHIKSAVIYSAYPLTDKQVGELAQMLNKRFDSELKISVEIEPELIGGIKVEVGDQVLDLSVQGKLSALYTTMTN | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19524
Sequence Length: 177
Subcellular Location: Cell inner membrane
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Q2GER4 | MQQYIAGRYAQSLYAVCGPRLESDANKFLGLLSENNFLSFAKVKTSTKLHVLDRLHLPCELKNLCKLLLANHRGFLCTTVLLGYIEIVKKNRKEADARVESYSRLSATAKKEVADALLIKFPYLKKINIAQKVNRSILGGLTIKINSIMIDLSIAGRLAKCKSIGQSTILEIFQ | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19443
Sequence Length: 174
Subcellular Location: Cell inner membrane
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Q4L7Y7 | MANVANKYAKALFDVAIDKDRLDLMYDELSEVSEATKNYGEDLRAIDSNPNQPASERRKFVGIVFGDANYYLKNMLMILANNRHLVLINSIFKEFKSLYNEYHNEDSAIVESVYQLSDEELDRIKDLILKQTNLSQVHITTKINPELIGGFRVKVGTTVLDGSVKKDLEQIERKFRRVN | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20591
Sequence Length: 179
Subcellular Location: Cell membrane
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Q49Z53 | MANIAKKYAKALFDTAKDADILDDMYDEFSTINEAVQSENKKLQALDADPQKDVEQRRRFVSIVFGQTNQYLQNMLTILASNRHLGHIHEIYIAFETLYNEEHNQDYAVIESVYQLSEEELSSIEEIIKARTKLSKIMITNKINPELIGGIRVKVGTKVMDASIKNDLAQLERQFIRVK | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20595
Sequence Length: 179
Subcellular Location: Cell membrane
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Q8E5V1 | MNKKTQALIEQYSKSLVEVAIEHKIVEKIQQEVAALIDIFETSELEGVLSSLAVSHDEKQHFVKTLQTSCSTYLVNFLEVIVQNEREALLYPILKSVDQELIKVNGQYPIQITTAVALSPEQKERLFDIAKTKLALPNGQLVEHIDPSIVGGFVVNANNKVIDASVRNQLHQFKMKLK | Function: 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20023
Sequence Length: 178
Subcellular Location: Cell membrane
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P07678 | MKTIHVSVVTPDGPVYEDDVEMVSVKAKSGELGILPGHIPLVAPLEISAARLKKGGKTQYIAVSGGFLEVRPDNVTILAQAAERAEDIDVLRAKARKSGRTPLQSQQDDIDFKRAELALKRAMNRLSVAEMK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14334
Sequence Length: 132
Subcellular Location: Cell membrane
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P37812 | MKTVKVNIVTPDGPVYDADIEMVSVRAESGDLGILPGHIPTVAPLKIGAVRLKKDGQTEMVAVSGGFVEVRPDHVTILAQAAETAEGIDKERAEAARQRAQERLNSQSDDTDIRRAELALQRALNRLDVAGK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14209
Sequence Length: 132
Subcellular Location: Cell membrane
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Q6G1X0 | MENNRVNHFLFELVSPEKPVFSEQVVSVVLPSASGALTVMANHAPLVASIVLGSMYVLTSSGEKLFAVCGGVANITSSGCSVLVERVVVVQHLSFHDLEQRILRVRATLEGDSNDGISHKIEDFFHQLKVGDAGLTEA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14818
Sequence Length: 138
Subcellular Location: Cell inner membrane
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Q6MGM8 | MNMKLTIVTPEKRILVGQEVDEVTVPAFKGELNILPGHAPLITTLETGVMKWKLKGKEKQDLAVISWGYCQVSPEGVNILANIADLPEEIDLQATKEFLALSEKKIMNELITDEDWAEFQRDWAHARAKIEAAEQQPAKK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15737
Sequence Length: 140
Subcellular Location: Cell inner membrane
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Q06J28 | MKLKVKIAIPGKVVWENEVDEVNIQTTTGKIGILPNHAPIIATVETSVLRMKSDESQNPILMVISDGYLSLEKNSIFIATDRCILEDNINASKLEEDYKTALERYNNAEKPGKKYIANKALKRINACYEILSYRNND | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15472
Sequence Length: 137
Subcellular Location: Plastid
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Q74GX9 | MAEKLKVDLVTPYKKILSEEVDEITATGALGEFSVLPGHAPFLTSLKIGELTYKKSGQIVHLALNWGYFEVEDDKVTVLVETAERADEIDLERAKAALGRAEAALKKLSPEDKDYRVMEAALERALIRMQVAGKAARK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15243
Sequence Length: 138
Subcellular Location: Cell inner membrane
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Q7NHG9 | MALQIKIVAPNKVVFDDQVDEVVLPSVSGQLGILTNHAPLITGLSNGVMRVRKQGTFIPIAVLTGVAEVDNNEVSVVAMAAELGSGIDVDRARAALARAEQTLATSQNKTELLQAQTALERANARLRAAGAL | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13825
Sequence Length: 132
Subcellular Location: Cell inner membrane
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A9H9B1 | MMPIKVEIVSPEKVLFSRAVDMALIPGLEGDIAAMPDHAPMMLLLRGGVVELHQDGAVTDRFFVAGGFADMTETSCTILADQATALSDLSVEAAQARLAELEASYDKADKMNVPVLDLLMAKMQSARAEIEAAGGPAVQGA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14830
Sequence Length: 141
Subcellular Location: Cell inner membrane
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Q0BQE9 | MAQTSLEIVSPEKRLLSRSVDMVVIPAAEGELGVLPGHAPMIVLLQGGTIRLYQNGQVTDRLYVAGGFAEITPERCTVLADQARPVAEISATEAEKRLADAEAAYATVDKLDITALDAAMESIQAARAMVEAARH | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14358
Sequence Length: 135
Subcellular Location: Cell inner membrane
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O78492 | MSIHISIIAPDRTVWDANAEEVILPSSTGQLGILKGHAPLLTALDIGVMRVRVDRDWTPIVLLGGFAEIENDELTILVNGAEEASQIDRDQAQRDLEEMTVKFNEATTNKERIEATQNLRKARARLQAVSA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14473
Sequence Length: 131
Subcellular Location: Plastid
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P84559 | QIIEANLALRR | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 1297
Sequence Length: 11
Subcellular Location: Plastid
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Q7VA75 | MSLTLRVLAPDKSVFDDTVEEVILPSTTGLLGILPGHISMVTAIDIGVLKLRSSNGNWDSIALMGGFAEVESDDVTVLVNAAELGKSIDKATAEKEFEQAKAALNKLEDQAGNSADKLKAKESLNKARARSQAVGE | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14367
Sequence Length: 136
Subcellular Location: Cellular thylakoid membrane
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Q82J85 | MAAELHVELVAADRQVWSGEATLVVARTTSGDIGVMPGHQPLLGVLESGPVTIRTSDGETVVAAVHGGFISFADNKLSLLAEIAELADEIDAQRAERELERAKAEGDATAERRADVRLRAVSAR | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13129
Sequence Length: 124
Subcellular Location: Cell membrane
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P0A2Z6 | MAAELHVALVAADREVWSGEATLVVARTTSGDIGVMPGHQPLLGVLESGPVTIRTSDGGTVVAAVHGGFISFADNKLSLLAEVAELSDEIDVHRAERKLEQAKTEGDAHAERRADVRLRAAAGR | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13018
Sequence Length: 124
Subcellular Location: Cell membrane
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Q04N64 | MAQLTVQIVTPDGLVYDHHASYVSVRTLDGEMGILPRHENMIAVLAVDEVKVKRIDDKDHVNWIAVNGGVIEIANDMITIVADSAERARDIDISRAERAKLRAERAIEEAQDKHLIDQERRAKIALQRAINRINVGNRL | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15638
Sequence Length: 139
Subcellular Location: Cell membrane
|
Q9TM29 | MQDILNIYLSSEESGGLFDFDATLPLMASQFLLIMLILDITFYKPINKVLKDRENYILKTLESATQISEKTKETLARYEEVILKSKKESQQLIDSIKTKTEHDIVNELIQTQNSTREFISKSIKELYRKKEQTLKVLEEDTENLSDKIYLKLINPKQ | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18351
Sequence Length: 157
Subcellular Location: Plastid
|
Q85FR1 | MSTGLFDFNGTLPVMGLQVVLLSWLLEQILYSPIQGVIQKRQNKIQQELQLAADQLQKAQQLTQEYQTQLQKAREKARERIRQVQQEAQTMMEDQLKQAQQQMTQLFNEAMQQLEQQKQQALMNLSNQVDEVAKFILSKLMKQ | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16721
Sequence Length: 143
Subcellular Location: Plastid
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P48085 | MTQWIIWLAIETEAAKPEGGLFDFDATLPVMMVQLLVLMLILNAVFYKPLIKILDERKEYIQSNFNEAEKCLAQAAELTTQYETKITDARQNASKLTNTTRSEIQRFVSEKLEEAQKKADSELASATNKLELQKDEALKSLESEVQTLSTKILEKLLGIQIANT | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18568
Sequence Length: 164
Subcellular Location: Plastid
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A8ZVQ5 | MRKNNGIKWWGWVTLSVLVMVAGDGTLAFAQETGGSAGWRPVYDNVMLVINFLILVFLLAKLLKNPLKNFLKTRHDEVAKELERLETERERAANDVADTKKQVAAEGTHILEIRERIIAEGERTKLAIIENAKKESEFLIEAARRRIQGRFQEARQAFRSELIESAMSIVSRRLPQEIGPQDQARQVDLFFTSLDQAQSKFSSARSASR | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23754
Sequence Length: 209
Subcellular Location: Cell inner membrane
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A8LKH8 | MATEATGAVEAAPGMPQLDFSTFPNQIFWLIITLVAIYLILTKVALPRIGSVLAERSGTITNDLAAAEELKLAAVEAEKAYNQALADARAEAQKIVAEARAEIQADLDVATAKADAEIAAKSAEAEKAIAEIREGAMASVTEVATDTAQALVAALLPSAKDADVSAAVAERVKG | Function: 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 (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17961
Sequence Length: 174
Subcellular Location: Cell inner membrane
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P35012 | MQYQYINSYSLLAAGGLFDFDATLSFIALEFLLLTSVLNLIYYQPISKVIDSREDYIRENLNKASLYLDQANELTKKYELELITARKEAIKMVTTSQTEAQEFVNAQISQAQKEAQQLIQSSMMQFEKEKNKAIYSLEKQVEQLSEQIKNKLISIYI | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18186
Sequence Length: 157
Subcellular Location: Plastid
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Q7NCS0 | MDMLFDPGWAAHLLLLAAEEAAAAEAESGGLFDFGGTLVLQIVNFLLLMTILSAVFYGPISRVIEERSEYIRSNAGSAQRRFDEAKALADQYEQELRTTRLEAQQVIAAAEAEAQKIRAQQLAEAQREAQERIAQAQADLDKQKQAALASLSGEVEAISRTLSEKLLSDSARRF | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19100
Sequence Length: 174
Subcellular Location: Cell inner membrane
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Q5FNY7 | MTVDWWTIGLQVINVSVLIWLLSRFFWRPICAVISRRQQEIAAQLAQVTDGQKQLEADRAAVKEARSSFEQERARIVQQAQQEAQSERQAILAKAQQDAAALEAGAKQSIAQEEAENQARWRSDAAALSCDIAGQLLAQTGCCRPARETLFDRLLKAIATLPDRERLSLRDGFTFATATAPSPDERQAYESALMTAVGEHPVITWAVDPALVEGFAVKTPYLTVASNWQADLVRIREGLSHAGH | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26966
Sequence Length: 244
Subcellular Location: Cell inner membrane
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Q0BQY4 | MQAHELSGAPWHHPVFWVAVAFVLFFVLFGRKIWGALTSKLDSYADEVRQNLDEARKLRREAEAMLEDARRRKEQALAEAKRLLESAHAEAARAAQALSDDAEASIRRREKMANDRIAAAEKAAVDEVRFAAADIASRAAKDILAREFGPYADAALIDSAISKLPQALRAA | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18910
Sequence Length: 171
Subcellular Location: Cell inner membrane
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O78478 | MTNYLYILALQIAEAESEGGLFDFNATLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQLIS | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18329
Sequence Length: 163
Subcellular Location: Plastid
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Q0AK30 | MMIRAEDAGHGEEQTLLEWLAAQPGDPSFYAFLALLIFFGLLLHMGVHRTIAKTLDDRAEGISNELDEAKRLREDAAEMLASYQRKQREAEAEAEAIIAQAKTEAKSLKAEARKEMTERLERRTAMAEQRIAQAEAQAAADVKAAAAELAAQAAEEILKTQLKKSDLNKLVDADIKTVGQRLN | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20217
Sequence Length: 183
Subcellular Location: Cell inner membrane
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Q603U6 | MDLNPSTFVLEIVNFLVLVWLLKRFLYQPVSAAIEERRRQIARTVAEARDTQTAAETLRMQYESRLADWESEKRQAREAFKQEIEAERQRALDELEKALDAEREKARVLIERQRRDMESDLERQALRLSRQFASRFLERLAGPEMEAALLRMFGEDLAAMSPEQWQALTRALEEQEHPEAEIASAFPLKPESCAELTEMIEARTGRAVAWRFREDPALICGIRLRAGHRVLAANVGEELKFFADGAENSLGGG | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 29045
Sequence Length: 253
Subcellular Location: Cell inner membrane
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B1ZJN3 | MAEQNILTTPSPNADTTIVPPGSPHTHTEQPSGGHGGAFPPFESHTFLAQLIWLALAFGLLYYLMSKVALPRIEAILGDRAGRLSSDLNEAQRMKAEADAAGAAYETSLREAQAKAQAIAQETRNSLSAEADAKRKTLEAELNQRLAASEATIRARTSEAMGNVRTIAGETASAIVERLTGQAPDQASLNRALDATPAVH | Function: 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 (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21184
Sequence Length: 200
Subcellular Location: Cell inner membrane
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Q8RC19 | MKEGKALELFNLSTFVFTIINLLVLYYILKRLLFKPVTKFLEDRENKIKSALEDADKQREEAYSLKAQYEEKLQNAENEGRAIIEKAQKEAEERASEIIKSANKEAESIIEKAKEEAVLEKIKAMHELRAEMSHLIIEAASKVLEKKLPVEDEDLIKEVIEEAGSWNK | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19379
Sequence Length: 168
Subcellular Location: Cell membrane
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A4XKX4 | MFDLAIFENMFFWAIINFLILYLIYRKFFFKKVTAFMEKRSKMIQEQLDFAAKSKEEAIKLKEEYENILSQAHAKANEIVQNAMIEAQKQADKIIEDAKLEANKIIENALKQLDIEKKKQINELKNQFVSIALLAASKVIEKNLNTEENRKIVENIFDEAGVA | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19009
Sequence Length: 163
Subcellular Location: Cell membrane
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A7ZC33 | MKIKILFFLALPFLAYASEHGGTNYDIVERTLNFLLFFAILVYFAAKPLKALYQSRIDRIANKLESIQEKLRESKAKKDDVLKRVEEAKQNANALIETAKKEAVNLAAKVKKEAQNDIANIEKGYKEQKEFEERKMTKGVVNEILSDIFSSDSLKVDQKELVNIILKKVS | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19440
Sequence Length: 170
Subcellular Location: Cell inner membrane
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A7I173 | MNKFLFFIFVFVGISFAGDDTATKDYDIVWRTINFAIFFGILFYLIKGPIKNAYNARINRISSRLEAIQTKLKESKEKKEASKKNLEDVKQKCVELIETAKKEAIQLDEKIQQSAQIDIAQMQKSFAEQKEFEIRRLKKSVTAEILDELFNEKSVNLSQNELINLVQKKVV | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19847
Sequence Length: 171
Subcellular Location: Cell inner membrane
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Q3A942 | MHFDWSDFIWTLINFFVLLFILKILLYKPVLKTIEDRKKSIEESLEKAAKAQEEAERIKAEYDGMIAKAREEAREIIAKAQKTAQAEKEEIIATAQREAQSLLADAKATIAQEKEKALRELRQEIGNLAVLAAGKILNRAVTLEDHQKLVDEFLNEVKM | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18210
Sequence Length: 159
Subcellular Location: Cell membrane
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P56086 | MFVVKMVLGFLILLSPLCATGLDISQTDIIERSLNFLLFVGILWYFSAKKLRSFLRSKSLEISKRLEEIQAQLKVSKENKKKLLKELEQAKEKAELIVSDANKEAYMITQKYELQTKMDVENLIKNSKALMDLEVKKIKRELVESVFKDLRESKKVSFNAQDCVNILKQRL | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19861
Sequence Length: 171
Subcellular Location: Cell inner membrane
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A9AVV0 | MDKLGVDLPLLISQIVNFCLLAFLLNTFLYKPVLNALQARSERIRESLDNAEKVKQQLARVDADYEAKLQEARREGQTIISQAQERARAQEAELLVVARNNAAKIEEEARGKVEQERQQVLRGLQGQLASLVTETASNVLGRELQTKGHDELINKSIDQLGRLN | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18445
Sequence Length: 164
Subcellular Location: Cell membrane
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B2XT88 | MENLTNIFLFLSNENEGIQLNTDIFEANIINLALLIVLVINVAKDVLGSILSARKASILDKIEEADKKLNEADKRFTEARLQWSQANIFGEDLEKKTYQRINAFHESQNLKNKDALLREYFSTLVVLDLKNEQVQKQVRNYVMELALIEVYGVFTKLVANKKFQENYSNYSVLLLEKLIGEK | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21003
Sequence Length: 182
Subcellular Location: Plastid
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Q0C0X0 | MKKTTSLLIAALAVAPLAHAAEGGFVGGLMYAATDPVTFVAFLCMVTFLLIAARMGAFKTILGGLDTRASNIRKELEEAASLREQAAEALALAERRAQDADKEAEAIIDQAKRDAKAMLEEARRDLAEKISRREAQAAARITRAETEATSEVRRAAADAATAAARRILSEQTSVDQFEAAARDIERALS | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20218
Sequence Length: 189
Subcellular Location: Cell inner membrane
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A8Z5R3 | MTPSLGLIFWQSVIFLISFIILSKFAWNPINKLLEKREKYIIDSINNAEKAKEYLKNIKLKKKNILKNTEKMKYFIINEAFKKKEQIEKEAKKKAKLESYLIINKTQLLIENKKKIAIEKIKNEILNMSIIISEKILNKELEINEKNNNYFFNKKLLIIMKFSYKIFIKRYAKGFFFLVFNSKKEIFIKNEIEKFFSYKKELYKKNYFKFKYTFFKKKRKDNFF | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27372
Sequence Length: 224
Subcellular Location: Cell membrane
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B2A3G6 | MVDPNLVTFVLTIVNILVLFYLLKRFLFKPIGEFMENRKNEIKQNLEDAEKERQEAEKLKEQYYEKLRGAKSEAQEIIQQARQREEEIIKEAKQEAKQEADDMIARAREEINQEQKKAIESLRSEVSDLTIQITERVLNDTIDKDQQKKLVQKYLKEVGRVS | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19184
Sequence Length: 162
Subcellular Location: Cell membrane
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Q9TL15 | MFHFLALTPLAHSEGFGLNTNILETNILNLAAVFALLAYVGTDFVSSLLKTRKESILKSLRDADERYQDAVNQLKQALQELETARTNAAEIRRQSEINAEAIRQRLELLTQEEMARLEEAKETIIKLEEEKAVAEVCTKVISMALVRAEKKIISSMDEAMHRRVMDMYLNLLREVY | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20113
Sequence Length: 176
Subcellular Location: Plastid
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Q3J6M7 | MNVTVTLIGQMVAFGILVWFVNRFLWGPLTNLMEERKKRVADGLAAAERGKHERELAEKRAKETLHEAKEKAAEIITQAQKRAGEIIEEAKEAAQAEGERLKVSANAEIQQEMNRAREDLRGQVVSIAVAGASKILKRELDEKANEALVKELVAQI | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17384
Sequence Length: 156
Subcellular Location: Cell inner membrane
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A6Q4C4 | MKQKLLMLLLLGSVSLFANEAAASGGTDIIPRTVNFLIFAAILYYLAAEPIKRFFQERKEGIAKRLEEVEAKLKEAKEEKAQAEAELKKAKELAQEIVETAKQEIEILTKEIKEQAKQEIEMLEKSFEESMELEKRKRVRAITKEVLEELFEEKALELEKEKFVNLIVKKVA | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19797
Sequence Length: 172
Subcellular Location: Cell inner membrane
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Q5Z0Y5 | MYEYSVLAAESGEDVNPLIPATYDIVWSVVCVAIIAVVFYKYVIPRLTKVLNERADKIEGGIAKAEAAQAEAQQTLEQYQQQLADARLEAARIREDARTQGQQILAQMRAEAQAESDRIVAAGHAQLEAQRQQILTELRSEVGRTAVDLAEKIIGQSVSDEAKQAASIERFLSELDSSDAGIGVGR | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20317
Sequence Length: 186
Subcellular Location: Cell membrane
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P12407 | MGTFLLLMAEASAVGGELAEGGAEGGFGLNTNILDTNLINLAIIITVLFVFGRKVLGNTLKTRRENIETAIKNAEQRAADAAKQLKEAQQKLEQAQAEAERIKKSAQDNAQTAGQAIIAQAAVDIERLQEAGAADLNAELDRAIAQLRQRVVALALQKVESELQGGISEDAQKTLIDRSIAQLGGGV | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19773
Sequence Length: 187
Subcellular Location: Cellular thylakoid membrane
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P95785 | MSTLINGTSLGNLLIVTGSFILLLLLVKKFAWSQLAAIFKAREEKIAKDIDDAENSRQNAQVLENKRQVELNQAKDEAAQIIDNAKETGKAQESKIITEAHEEAGRLKDKANQDIATSKAEALSSVKADVADLSVLLAEKIMAKNLDKTAQGDLIDSYLDKLGDA | Function: 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17922
Sequence Length: 165
Subcellular Location: Cell membrane
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A9WGS5 | MPSSREIKRRIRSVKNVAQITRAMEMVSASKMRRAQRNVLATRPYADRMREVMANLTARVVGAARRGTLLEKRETVKSVALLVVTPDRGLCGSLVANVLRRAGRFITEQRAMGRTVDVYTFGRKGRDFFLRTGFAPAGEATRLGDAPKLEAILGVAISAINGFQSGKYDELYIIYSEFINTLVQRPAIKQLLPVESPDISTTTNVDYTYEPGEEEVLNSILPRYVETQIYQAVLESIASEHSARMVAMRNATNNAKDLVRDLTLSFNKARQAAITKEVSEIASGAAALTS | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32075
Sequence Length: 290
Subcellular Location: Cell membrane
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