Function and Biology Details
Reaction catalysed:
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
- Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal
- Beta-lactamase/transpeptidase-like
- D-Ala-D-Ala carboxypeptidase, C-terminal domain superfamily
- Penicillin-binding protein, C-terminal domain superfamily
- Peptidase S11, D-alanyl-D-alanine carboxypeptidase A, N-terminal
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
D-alanyl-D-alanine carboxypeptidase DacA (preferred)
PDBe Complex ID:
PDB-CPX-155177 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanyl-D-alanine carboxypeptidase DacA
Molecule details ›
Chain: A
Length: 344 amino acids
Theoretical weight: 37.99 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 344 amino acids
Theoretical weight: 37.99 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
- Canonical:
P44466 (Residues: 30-373; Coverage: 92%)
Sequence domains:
Structure domains:
