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atp-2

Gene
atp-2
Protein
ATP synthase subunit beta, mitochondrial
Organism
Caenorhabditis elegans
Length
538 amino acids
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. Required during male mating behavior for the response to hermaphrodite contact, acting with lov-1 and pkd-2. May be involved in polycystin signaling.
Similarity
Belongs to the ATPase alpha/beta chains family.
Mass
57.527 kDa
Sequence
MASRSLASISRSASRLLQSNVQKCALPAASIRLSSNNVESKKGIHTGVATQQAAAATKVSAKATAANASGRIVAVIGAVVDVQFDENLPPILNGLEVVGRSPRLILEVSQHLGDNVVRCIAMDGTEGLVRGQPVADTGDPIKIPVGPETLGRIMNVIGEPIDERGPIASKNFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIEGGVIDLKGKNSKVSLVYGQMNEPPGARARVCLTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRGIAELAIYPAVDPLDSTSRIMDPNVVGQNHYDIARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHQGKFVSLEETIRGFTMILKGELDHLPEVAFYMQGGIDDVFKKAEELAKQHGN

Gene
atp-2
Protein
ATP synthase subunit beta, mitochondrial
Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Length
519 amino acids
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.
Similarity
Belongs to the ATPase alpha/beta chains family.
Mass
55.533 kDa
Sequence
MFKSGISAFARTARPSFAAASRRAVRPAALNLRAPALSRFASSAGVGDGKIYQVIGAVVDVKFDTDKLPPILNALETQNNGQKLVLEVSQHLGENVVRCIAMDGTEGLVRGAKASDTGAPITIPVGPATLGRIINVTGDPIDERGPIKTDKFRPIHAEAPEFVEQSTTAEILVTGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGYSVFTGVGERTREGNDLYHEMQETSVIQLDGDSKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLAVDMGQMQERITTTTKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRMLDPRIVGQEHYETATRVQQILQEYKSLQDIIAILGMDELSEADKLTVERARKIQRFLSQPFTVAQVFTGIEGKLVDLKDTIASFKAILAGEGDDLPEGAFYMVGDFASARAKGEKILAELEGQA