Family

ATPase, F1 complex, beta subunit (IPR005722)

Short name: ATPase_F1-cplx_bsu

Family relationships

None.

Description

This entry represents the beta subunit found in the F1 complex of F-ATPases.

F-ATPases (also known as F1F0-ATPase, or H(+)-transporting two-sector ATPase) (EC:3.6.3.14) are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), nine in mitochondria (A-G, F6, F8). Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits, while in the F0 complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the F0 rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis [PMID: 11309608]. These ATPases can also work in reverse in bacteria, hydrolysing ATP to create a proton gradient.

In F-ATPases, there are three copies each of the alpha and beta subunits that form the catalytic core of the F1 complex, while the remaining F1 subunits (gamma, delta, epsilon) form part of the stalks. There is a substrate-binding site on each of the alpha and beta subunits, those on the beta subunits being catalytic, while those on the alpha subunits are regulatory. The alpha and beta subunits form a cylinder that is attached to the central stalk. The alpha/beta subunits undergo a sequence of conformational changes leading to the formation of ATP from ADP, which are induced by the rotation of the gamma subunit, itself is driven by the movement of protons through the F0 complex C subunit [PMID: 12745923, PMID: 11533724].

GO terms

Biological Process

GO:0015986 ATP synthesis coupled proton transport

Molecular Function

GO:0046933 proton-transporting ATP synthase activity, rotational mechanism

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
TIGRFAMs
PANTHER
HAMAP