ATP2

ATP synthase subunit beta, mitochondrial

574 amino acids

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.

Belongs to the ATPase alpha/beta chains family.

61.821 kDa

MLSSVRLAALRAGKTNSVFQAVRAFAAEPAAAATTDAGFVSQVIGPVVDVRFDGELPSILSALEVQGHNVRLVLEVAQHMGDNTVRCVAMDSTDGLVRGQKVVNTGSPIKVPVGRGTLGRIMNVIGEPVDEQGPIECSEVWSIHREAPEFTEQSTEQEILVTGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKLGDKRGESKCTLVYGQMNEPPGARARVALTGLTVAEYFRDVEGQDVLLFVDNIFRFTQANSEVSALLGRIPSAVGYQPTLATDLGGLQERITTTTKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRSIAELGIYPAVDPLDSTSRMLNPNIIGAEHYNIARGVQKVLQDYKNLQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFQVAEVFTGTPGKYVDLKDTISAFTGILQGKYDDLPEMAFYMVGGIHEVVEKADKLAKDVAARKDESKKAKSSEALKDVPSLEKMAGEIKDEVIDADDSLEEDFKAEAISSENMVLNEKGEKVPLPKK

atp2

ATP synthase subunit beta, mitochondrial

525 amino acids

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.

Belongs to the ATPase alpha/beta chains family.

56.876 kDa

MLKKQALSGIRRFSLATKQSFVKTSYKLPRKSWLNTAKFNTIRYASTEAAKHNKGSIKQVIGAVVDCQFEDADSLPSILNALEVKLPDNKRLVLEVAQHVGENTVRTIAMDGTEGLVRGTAVIDTGSPISIPVGPGTLGRIMNVIGEPVDERGPIKAVKYSPIHADAPSFEEQSTTPEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGYSVFTGVGERTREGNDLYREMQETGVIKLEGESKAALVFGQMNEPPGARARVALTGLTVAEYFRDIEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGAMQERITTTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRSISELGIYPAVDPLDSKSRMMDPRILGEEHYNLAGSVQQMLQEYKSLQDIIAILGMDELSEADKLTVERARKVQRFLSQPFAVAEVFTGIEGRLVSLKDTIRSFKEILEGKHDSLPESAFYMVGSIDDAVKKAEKIAQELAA

ATP2

ATP synthase subunit beta, mitochondrial

511 amino acids

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.

Belongs to the ATPase alpha/beta chains family.

54.794 kDa

MVLPRLYTATSRAAFKAAKQSAPLLSTSWKRCMASAAQSTPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN

ATP2

ATP synthase subunit beta, mitochondrial

509 amino acids

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27373333). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (PubMed:27373333). Subunits alpha/ATP1 and beta/ATP2 form the catalytic core in F(1) (PubMed:27373333). 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 (PubMed:27373333).

Belongs to the ATPase alpha/beta chains family.

54.535 kDa

MVLPRLIPRLSRSAFKVAQANNRVFNAPFRGMASSAGVGSGKIRTVIGAVVDVQFEQDNLPAILNALTIDRGEGNKLVLEVAQHLGENTVRTIAMDGTEGLVRGTSVADTGAPITIPVGRGTLGRIINVCGEPIDERGPIEATKFLPIHADPPTFAEQSTTAEVLETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFCGVGERTREGNDLYREMKETGVINLEGESKVTLVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGALQERITTTQKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDIDVVGQEHYDVASNVQQTLQAYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFTVAEVFTGIEGRLVSLKDTVRSFKEILDGKHDALPEAAFYMVGGIEEVVAKAEKLAAESK

ATP2

ATP synthase subunit beta, mitochondrial

505 amino acids

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.

Belongs to the ATPase alpha/beta chains family.

54.069 kDa

MVLPRFYAASSRAALQAARRAVPFTGVRGYAAAASSQGKVRAVIGAIVDVQFEQGQLPAILNALEIDTPEGKLVLEVAQHLGENTVRTIAMDGTEGLVRGENVSDTGAPISVPVGRETLGRIINVIGEPIDERGPINSKMRKPIHADPPLFVEQSTAAEVLETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGDSKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVATQVQQTLQAYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGRLVRLKDTISSFKAVLDGKYDHLPENAFYMVGGIEDVVAKAEKLAAEAN

ATP2

ATP synthase subunit beta, mitochondrial

476 amino acids

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27791192). 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). Subunits alpha/ATP1 and beta/ATP2 form the catalytic core in F(1) (By similarity). 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 (By similarity).

Belongs to the ATPase alpha/beta chains family.

50.803 kDa

ATAGPASGKIRAVIGAVVDVQFEQGELPAILNALTIDQGNNQKLVLEVAQHLGENAVRAIAMDGTEGLVRGQTVVDTGAPISVPVGRGTLGRIINVVGEPIDERGPIECKQRNPIHADPPSFVEQSTEAEVLETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTRKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDVSVVGQEHYDVATGVQQTLQAYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIEGKLVRLKDTIASFKAVLEGKYDHLPENAFYMVGGIEDVVAKAEKIAAEAN

atp2

ATP synthase subunit beta, mitochondrial

114 amino acids

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.

Belongs to the ATPase alpha/beta chains family.

12.033 kDa

multiple

KVHQVIGAVVDVKFRVPVGAGTLGRIINVTGDPIDERGKIGLFGGAGVGKTKVALVFGQMNEPPGARARFTQAGSEVSALLGRMRGISELGIYPAVDPLDSKSRVQQMLQEYKS