MitoProteome Database

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MT000051

UniProt Annotations

Entry Information

Gene Name	ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide
Protein Entry	ATPB_HUMAN
UniProt ID	P06576
Species	Human

Comments

Comment type	Description
Catalytic Activity	ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
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.
Interaction	P63104:YWHAZ; NbExp=2; IntAct=EBI-356231, EBI-347088;
Similarity	Belongs to the ATPase alpha/beta chains family. {ECO:0000305}.
Subcellular Location	Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein.
Subunit	F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68. Interacts with PPIF. Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP synthase and enhances neurons metabolic efficency (By similarity). {ECO:0000250}.