The domain within your query sequence starts at position 2 and ends at position 69; the E-value for the ATP-synt_E domain shown below is 6.3e-18.
VPPVQVSPLIKFGRYSALIIGMAYGAKRYSYLKPRAEEERRIAAEEKKRLDELKRIEREL AEAQDDSI
ATP-synt_E |
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PFAM accession number: | PF05680 |
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Interpro abstract (IPR008386): | 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:
F-ATPases (also known as ATP synthases, F1F0-ATPase, or H(+)-transporting two-sector ATPase) ( EC 3.6.3.14 ) 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), with additional subunits in mitochondria. 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 [ (PUBMED:11309608) ]. These ATPases can also work in reverse in bacteria, hydrolysing ATP to create a proton gradient. This entry represents subunit E found in the F0 complex of F-ATPases. Mitochondrial F-ATPases can associate together to form dimeric or oligomeric complexes, such interactions involving the physical association of membrane-embedded F0 complexes. In yeast, the F0 complex E subunit appears to play an important role in supporting F-ATPase dimerisation. This subunit is anchored to the inner mitochondrial membrane via its N-terminal region, which is involved in stabilising subunits G and K of the F0 complex. The C-terminal region of subunit E is hydrophilic, protruding into the intermembrane space where it can also help stabilise the F-ATPase dimer complex [ (PUBMED:15701797) ]. |
GO process: | ATP synthesis coupled proton transport (GO:0015986) |
GO component: | mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) (GO:0000276) |
GO function: | proton transmembrane transporter activity (GO:0015078) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry ATP-synt_E