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:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Penicillin-binding protein 1A (preferred)
PDBe Complex ID:
PDB-CPX-170056 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Penicillin-binding protein 1A
Molecule details ›
Chains: A, C
Length: 24 amino acids
Theoretical weight: 2.64 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli
UniProt:
Length: 24 amino acids
Theoretical weight: 2.64 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli
UniProt:
- Canonical:
Q04707 (Residues: 47-70; Coverage: 3%)
Penicillin-binding protein 1A
Molecule details ›
Chains: B, D
Length: 390 amino acids
Theoretical weight: 43.57 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli
UniProt:
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily
Length: 390 amino acids
Theoretical weight: 43.57 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli
UniProt:
- Canonical: Q04707 (Residues: 264-653; Coverage: 54%)
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily
