Summary: ATP synthase (C/AC39) subunit
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ATP synthase (C/AC39) subunit Provide feedback
This family includes the AC39 subunit from vacuolar ATP synthase P32366  and the C subunit from archaebacterial ATP synthase . The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae P43456 .
Bauerle C, Ho MN, Lindorfer MA, Stevens TH; , J Biol Chem 1993;268:12749-12757.: The Saccharomyces cerevisiae VMA6 gene encodes the 36-kDa subunit of the vacuolar H(+)-ATPase membrane sector. PUBMED:8509410 EPMC:8509410
Wilms R, Freiberg C, Wegerle E, Meier I, Mayer F, Muller V; , J Biol Chem 1996;271:18843-18852.: Subunit structure and organization of the genes of the A1A0 ATPase from the Archaeon Methanosarcina mazei Go1. PUBMED:8702544 EPMC:8702544
Takase K, Kakinuma S, Yamato I, Konishi K, Igarashi K, Kakinuma Y; , J Biol Chem 1994;269:11037-11044.: Sequencing and characterization of the ntp gene cluster for vacuolar- type Na(+)-translocating ATPase of Enterococcus hirae. PUBMED:8157629 EPMC:8157629
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002843
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 (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 vacuoles and catalyse ATP hydrolysis to transport solutes and lower pH in organelles.
- 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.
The V-ATPases (or V1V0-ATPase) and A-ATPases (or A1A0-ATPase) are each composed of two linked complexes: the V1 or A1 complex contains the catalytic core that hydrolyses/synthesizes ATP, and the V0 or A0 complex that forms the membrane-spanning pore. The V- and A-ATPases both contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis [PUBMED:11309608, PUBMED:15629643, PUBMED:15168615]. The V- and A-ATPases more closely resemble one another in subunit structure than they do the F-ATPases, although the function of A-ATPases is closer to that of F-ATPases.
This entry represents subunit C from the A0 complex of A-ATPases, and subunits C and D from the V0 complex of V-ATPases, all of which are involved in the translocation of protons across a membrane. There is more than one type of D subunit in V-ATPases, where the D1 subunit is ubiquitous, while the D2 subunit has limited tissue expressivity, possibly to account for differential functions, targeting or regulation of V-ATPase activity [PUBMED:15800125].
More information about this protein can be found at Protein of the Month: ATP Synthases [PUBMED:].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||proton-transporting two-sector ATPase complex, proton-transporting domain (GO:0033177)|
|Molecular function||hydrogen ion transmembrane transporter activity (GO:0015078)|
|Biological process||ATP hydrolysis coupled proton transport (GO:0015991)|
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Curation and family details
|Seed source:||Enright A|
|Author:||Enright A, Ouzounis C, Bateman A|
|Number in seed:||10|
|Number in full:||1321|
|Average length of the domain:||301.60 aa|
|Average identity of full alignment:||22 %|
|Average coverage of the sequence by the domain:||94.11 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the vATP-synt_AC39 domain has been found. There are 5 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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