Function and Biology Details
Reaction catalysed:
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183320 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
histidine kinase
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 31.7 KDa
Source organism: Vibrio parahaemolyticus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
Length: 277 amino acids
Theoretical weight: 31.7 KDa
Source organism: Vibrio parahaemolyticus
Expression system: Escherichia coli
UniProt:
- Canonical:
Q87ID1 (Residues: 51-322; Coverage: 28%)
Sequence domains:
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
Periplasmic binding protein/LacI sugar binding domain-containing protein
Molecule details ›
Chain: B
Length: 304 amino acids
Theoretical weight: 33.89 KDa
Source organism: Vibrio parahaemolyticus
Expression system: Escherichia coli
UniProt:
Sequence domains: Periplasmic binding proteins and sugar binding domain of LacI family
Structure domains: Rossmann fold
Length: 304 amino acids
Theoretical weight: 33.89 KDa
Source organism: Vibrio parahaemolyticus
Expression system: Escherichia coli
UniProt:
- Canonical: Q87ID2 (Residues: 31-329; Coverage: 98%)
Sequence domains: Periplasmic binding proteins and sugar binding domain of LacI family
Structure domains: Rossmann fold
