Function and Biology Details
Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- P-loop containing nucleoside triphosphate hydrolase
- PD-(D/E)XK endonuclease-like domain, AddAB-type
- DNA helicase subunit AddA
- DNA helicase, UvrD/REP type
- PD-(D/E)XK endonuclease-like domain superfamily
- DNA helicase subunit AddB
- UvrD-like DNA helicase, C-terminal
- Restriction endonuclease type II-like
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
1 distinct DNA molecule
1 distinct DNA molecule
Macromolecules (3 distinct):
ATP-dependent helicase/nuclease subunit A
Molecule details ›
Chain: A
Length: 1232 amino acids
Theoretical weight: 141.22 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli B
UniProt:
Sequence domains:
Length: 1232 amino acids
Theoretical weight: 141.22 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli B
UniProt:
- Canonical:
P23478 (Residues: 1-1232; Coverage: 100%)
Sequence domains:
- UvrD/REP helicase N-terminal domain
- PD-(D/E)XK nuclease superfamily
- UvrD-like helicase C-terminal domain
ATP-dependent helicase/deoxyribonuclease subunit B
Molecule details ›
Chain: B
Length: 1166 amino acids
Theoretical weight: 134.77 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli B
UniProt:
Sequence domains:
Structure domains:
Length: 1166 amino acids
Theoretical weight: 134.77 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli B
UniProt:
- Canonical: P23477 (Residues: 1-1166; Coverage: 100%)
Sequence domains:
Structure domains:
