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:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
- Beta-lactamase/transpeptidase-like
- Penicillin-binding protein 4, C-terminal domain
- Peptidase S11, D-alanyl-D-alanine carboxypeptidase A, N-terminal
- Penicillin-binding protein 4, C-terminal domain superfamily
- Penicillin-binding protein, C-terminal domain superfamily
Structure analysis Details
Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanyl-D-alanine carboxypeptidase
Molecule details ›
Chains: A, B
Length: 453 amino acids
Theoretical weight: 50.68 KDa
Source organism: Staphylococcus aureus subsp. aureus COL
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 453 amino acids
Theoretical weight: 50.68 KDa
Source organism: Staphylococcus aureus subsp. aureus COL
Expression system: Escherichia coli
UniProt:
- Canonical:
A0A0H2WY27 (Residues: 1-431; Coverage: 100%)
Sequence domains:
Structure domains:
