InterPro : IPR000568

Name  ATPase, F0 complex, subunit A Short Name  ATPase_F0-cplx_asu
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.F-ATPases (also known as F1F0-ATPase, or H(+)-transporting two-sector ATPase) () 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 []. These ATPases can also work in reverse in bacteria, hydrolysing ATP to create a proton gradient.This entry represents subunit A (or subunit 6) found in the F0 complex of F-ATPases. This subunit is a key component of the proton channel, and may play a direct role in the translocation of protons across the membrane. Catalysis in the F1 complex depends upon the rotation of the central stalk and F0 c-ring, which in turn is driven by the flux of protons through the membrane via the interface between the F0 c-ring and subunit A. The peripheral stalk links subunit A to the external surface of the F1 domain, and is thought to act as a stator to counter the tendency of subunit A and the F1 alpha(3)beta(3) catalytic portion to rotate with the central rotary element[].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

1 Child Features

Id Name Short Name Type
IPR017692 Alternate F1F0 ATPase, F0 subunit A Alt_ATPase_F0_Asu Family

1 Contains

Id Name Short Name Type
IPR023011 ATPase, F0 complex, subunit A, active site ATPase_F0-cplx_asu_AS Active_site

0 Found In

0 Parent Features

8 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
Carbajo RJ Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. 2005 J Mol Biol 351 824-38



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)