InterPro : IPR024034

Name  ATPase, F1 complex beta subunit/V1 complex, C-terminal Short Name  ATPase_F1_bsu/V1_C
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.This entry represents a domain that is found in the C terminus of the F1 ATP synthase beta subunit and in the C terminus of the V-ATPase alpha and beta subunits.
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1 Parent Features

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

6 Publications

First Author Title Year Journal Volume Pages
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



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)