InterPro : IPR005724

Name  ATPase, A1 complex, beta subunit Short Name  ATPase_A1-cplx_bsu
Type  Family 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.A-ATPases (or A1A0-ATPase) () are found exclusively in Archaea and display a close resemblance in structure and subunit composition with V-ATPases, although their function in both ATP synthesis and ATP hydrolysis is closer to that of F-ATPases []. A-ATPases are composed of two linked complexes: the A1 complex consisting of seven subunits contains the catalytic core that synthesizes/hydrolyses ATP, while the A0 complex consisting of at least two subunits forms the membrane-spanning pore []. The rotary motor in A-ATPases is composed of only two subunits, the stator subunit I and the rotor subunit C []. A-ATPases may have arisen as an adaptation to the different cellular needs and the more extreme environmental conditions faced by Archaeal species.This entry represents the beta subunit from the A1 complex of A-ATPases. The A1 complex contains three copies each of subunits alpha (or A) (), and beta (or B), both of which form the headpiece that participates in nucleotide binding. However, only the alpha subunit is catalytic, the beta subunit being regulatory in function [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

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

1 Parent Features

Id Name Short Name Type
IPR022879 V-type ATP synthase regulatory subunit B/beta V-ATPase_su_B/beta Family

10 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
Müller V An exceptional variability in the motor of archael A1A0 ATPases: from multimeric to monomeric rotors comprising 6-13 ion binding sites. 2004 J Bioenerg Biomembr 36 115-25
Wilms R Subunit structure and organization of the genes of the A1A0 ATPase from the Archaeon Methanosarcina mazei Gö1. 1996 J Biol Chem 271 18843-52
Müller V Structure and function of the A1A0-ATPases from methanogenic Archaea. 1999 J Bioenerg Biomembr 31 15-27
Coskun U Three-dimensional organization of the archaeal A1-ATPase from Methanosarcina mazei Gö1. 2004 J Biol Chem 279 22759-64



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)