InterPro : IPR000194

Name  ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain Short Name  ATPase_F1/V1/A1_a/bsu_nucl-bd
Type  Domain Description  Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [, ]. The different types include:F-ATPases (F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases), which are primarily found in eukaryotic and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane []. They are also found in bacteria [].A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases, though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases [, ].P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.The F-ATPases (or F1F0-ATPases), V-ATPases (or V1V0-ATPases) and A-ATPases (or A1A0-ATPases) are composed of two linked complexes: the F1, V1 or A1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the F0, V0 or A0 complex that forms the membrane-spanning pore. The F-, V- and A-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis [, ].In F-ATPases, there are three copies each of the alpha and beta subunits that form the catalytic core of theF1 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 driven by the movement of protons through the F0 complex C subunit [].In V- and A-ATPases, the alpha/A and beta/B subunits of the V1 or A1 complex are homologous to the alpha and beta subunits in the F1 complex of F-ATPases, except that the alpha subunit is catalytic and the beta subunit is regulatory.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 []. This entry represents the central domain. It is found in the alpha and beta subunits from F1, V1, and A1 complexes, as well as in flagellar ATPase and the termination factor Rho.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

1 Contains

Id Name Short Name Type
IPR020003 ATPase, alpha/beta subunit, nucleotide-binding domain, active site ATPase_a/bsu_AS Active_site

14 Found In

Id Name Short Name Type
IPR005294 ATPase, F1 complex, alpha subunit ATPase_F1-cplx_asu Family
IPR005723 ATPase, V1 complex, subunit B ATPase_V1-cplx_bsu Family
IPR005722 ATPase, F1 complex, beta subunit ATPase_F1-cplx_bsu Family
IPR005725 ATPase, V1 complex, subunit A ATPase_V1-cplx_asu Family
IPR005714 ATPase, type III secretion system, FliI/YscN ATPase_T3SS_FliI/YscN Family
IPR005724 ATPase, A1 complex, beta subunit ATPase_A1-cplx_bsu Family
IPR005726 ATP synthase alpha chain, archaea ATPase_asu_arc Family
IPR013380 ATPase, type III secretion system, H+-transporting ATPase_T3SS_H-transp Family
IPR017691 ATP synthase subunit beta, bacterial and archaeal Alt_ATPase_F1_bsu Family
IPR017710 Alternate F1F0 ATPase, F1 subunit alpha Alt_ATPase_F1_asu Family
IPR022425 Flagellar export ATPase FliI, clade 2 FliI_clade2 Family
IPR004665 Transcription termination factor Rho Term_rho Family
IPR020005 Flagellar export ATPase FliI, clade 1 FliI_clade1 Family
IPR022426 Flagellum-specific ATP synthase FliI, clade 3 FliI_clade3 Family

0 Parent Features

10 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
Cross RL The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. 2004 FEBS Lett 576 1-4
Rappas M Mechanisms of ATPases--a multi-disciplinary approach. 2004 Curr Protein Pept Sci 5 89-105
Toei M Regulation and isoform function of the V-ATPases. 2010 Biochemistry 49 4715-23
Grüber G New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0). 2008 Bioessays 30 1096-109
Schäfer G F-type or V-type? The chimeric nature of the archaebacterial ATP synthase. 1992 Biochim Biophys Acta 1101 232-5
Radax C F-and V-ATPases in the genus Thermus and related species. 1998 Syst Appl Microbiol 21 12-22
Abrahams JP Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. 1994 Nature 370 621-8
Wilkens S A structural model of the vacuolar ATPase from transmission electron microscopy. 2005 Micron 36 109-26
Leyva JA Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review). 2003 Mol Membr Biol 20 27-33

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)