InterPro : IPR005722

Name  ATPase, F1 complex, beta subunit Short Name  ATPase_F1-cplx_bsu
Type  Family 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) () arecomposed 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 []. 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 [, ].
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

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0 Child Features

4 Contains

Id Name Short Name Type
IPR000793 ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal ATPase_F1/V1/A1-cplx_a/bsu_C Domain
IPR004100 ATPase, F1 complex alpha/beta subunit, N-terminal domain ATPase_F1_a/bsu_N Domain
IPR000194 ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain ATPase_F1/V1/A1_a/bsu_nucl-bd Domain
IPR020003 ATPase, alpha/beta subunit, nucleotide-binding domain, active site ATPase_a/bsu_AS Active_site

0 Found In

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Yasuda R Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. 2001 Nature 410 898-904
Leyva JA Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review). 2003 Mol Membr Biol 20 27-33
Yoshida M ATP synthase--a marvellous rotary engine of the cell. 2001 Nat Rev Mol Cell Biol 2 669-77



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)