Domain

ATPase, F1 complex alpha/beta subunit, N-terminal domain (IPR004100)

Short name: ATPase_F1_a/bsu_N

Domain relationships

None.

Description

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.

The structure of the alpha and beta subunits is almost identical. Each subunit consists of a N-terminal beta-barrel, a central domain containing the nucleotide-binding site and a C-terminal alpha bundle domain [PMID: 8065448]. This entry represents the N-terminal domain, which forms a closed beta-barrel with Greek-key topology.

GO terms

Biological Process

GO:0046034 ATP metabolic process
GO:0015992 proton transport

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam
SUPERFAMILY