Function and Biology Details
Reaction catalysed:
ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- V-ATPase proteolipid subunit
- F/V-ATP synthase subunit C superfamily
- V-ATPase proteolipid subunit C-like domain
- V-type ATP synthase regulatory subunit B/beta
- P-loop containing nucleoside triphosphate hydrolase
- ATPase, alpha/beta subunit, nucleotide-binding domain, active site
- ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
- ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain
19 more domains
Structure analysis Details
Assembly composition:
hetero 26-mer (preferred)
PDBe Complex ID:
PDB-CPX-131510 (preferred)
Entry contents:
9 distinct polypeptide molecules
Macromolecules (9 distinct):
V-type ATP synthase alpha chain
Molecule details ›
Chains: A, B, C
Length: 578 amino acids
Theoretical weight: 63.7 KDa
Source organism: Thermus thermophilus HB8
UniProt:
Sequence domains:
Length: 578 amino acids
Theoretical weight: 63.7 KDa
Source organism: Thermus thermophilus HB8
UniProt:
- Canonical:
Q56403 (Residues: 1-578; Coverage: 100%)
Sequence domains:
V-type ATP synthase beta chain
Molecule details ›
Chains: D, E, F
Length: 478 amino acids
Theoretical weight: 53.22 KDa
Source organism: Thermus thermophilus HB8
UniProt:
Sequence domains:
Length: 478 amino acids
Theoretical weight: 53.22 KDa
Source organism: Thermus thermophilus HB8
UniProt:
- Canonical: Q56404 (Residues: 1-478; Coverage: 100%)
Sequence domains:
V-type ATP synthase subunit D
V-type ATP synthase subunit F
V-type ATP synthase, subunit (VAPC-THERM)
V-type ATP synthase subunit E
V-type ATP synthase subunit C
V-type ATP synthase subunit I
V-ATPase proteolipid subunit C-like domain-containing protein
