Function and Biology Details
Reactions catalysed:
(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate
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 domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Penicillin-binding protein 1A (preferred)
PDBe Complex ID:
PDB-CPX-184168 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Penicillin-binding protein 1A
Penicillin-binding protein 1A
Molecule details ›
Chain: B
Length: 385 amino acids
Theoretical weight: 43.18 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli
UniProt:
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily
Length: 385 amino acids
Theoretical weight: 43.18 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8DR59 (Residues: 266-650; Coverage: 54%)
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily
