ATP-synt_E_2 |
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PFAM accession number: | PF08112 |
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Interpro abstract (IPR012508): | A-ATPases (or A1A0-ATPase) ( EC 3.6.3.14 ) 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 [ (PUBMED:10340845) ]. 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 [ (PUBMED:8702544) ]. The rotary motor in A-ATPases is composed of only two subunits, the stator subunit I and the rotor subunit C [ (PUBMED:15168615) ]. A-ATPases may have arisen as an adaptation to the different cellular needs and the more extreme environmental conditions faced by Archaeal species. 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 [ (PUBMED:15473999) (PUBMED:15078220) ]. The different types include:
The epsilon subunit is the smallest (7kDa) of those found in the A1 complex. Unlike the A, B and C subunits, the epsilon subunit does not have a homologous counterpart in F- or V-ATPases [ (PUBMED:2147683) ]. |
GO process: | ATP synthesis coupled proton transport (GO:0015986) |
GO component: | proton-transporting two-sector ATPase complex, catalytic domain (GO:0033178) |
GO function: | ATPase-coupled transmembrane transporter activity (GO:0042626) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry ATP-synt_E_2