Summary: ATP synthase I chain
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The atp operon of alkaliphilic Bacillus pseudofirmus OF4, as in most prokaryotes, contains the eight structural genes for the F-ATPase (ATP synthase), which are preceded by an atpI gene that encodes a membrane protein with 2 TMSs. A tenth gene, atpZ, has been found in this operon, which is upstream of and overlapping with atpI. AtpI is a Ca2+/Mg2+ transporter .
Santana M, Ionescu MS, Vertes A, Longin R, Kunst F, Danchin A, Glaser P; , J Bacteriol 1994;176:6802-6811.: Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and characterization of atp mutants. PUBMED:7961438 EPMC:7961438
Hicks DB, Wang Z, Wei Y, Kent R, Guffanti AA, Banciu H, Bechhofer DH, Krulwich TA;, Proc Natl Acad Sci U S A. 2003;100:10213-10218.: A tenth atp gene and the conserved atpI gene of a Bacillus atp operon have a role in Mg2+ uptake. PUBMED:12917488 EPMC:12917488
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005598
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 and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane [PUBMED:20450191]. They are also found in bacteria [PUBMED:9741106].
- 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 [PUBMED:18937357, PUBMED:1385979].
- 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) (EC) 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 [PUBMED:11309608]. These ATPases can also work in reverse in bacteria, hydrolysing ATP to create a proton gradient.
The atp operon of most prokaryotes contains the structural genes for the F-ATPase (ATP synthase), which are preceded by an atpI gene that encodes a membrane protein of unknown function. A possible function for this protein is to guide the assembly of the membrane sector of the ATPase enzyme complex [PUBMED:7961438]. A role in magnesium uptake has also been suggested [PUBMED:12917488].
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These two subunits from the F-type and N-type ATPases have been demonstrated to from functionally distinct components of these two different ATPases.
The clan contains the following 2 members:ATP-synt_I AtpR
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Curation and family details
|Number in seed:||97|
|Number in full:||12772|
|Average length of the domain:||92.80 aa|
|Average identity of full alignment:||29 %|
|Average coverage of the sequence by the domain:||74.11 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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