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:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Penicillin-binding protein 1A (preferred)
PDBe Complex ID:
PDB-CPX-130392 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Penicillin-binding protein 1A
Molecule details ›
Chain: A
Length: 200 amino acids
Theoretical weight: 22.91 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Transglycosylase
Structure domains: Biosynthetic peptidoglycan transglycosylase-like
Length: 200 amino acids
Theoretical weight: 22.91 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
O66874 (Residues: 51-243; Coverage: 27%)
Sequence domains: Transglycosylase
Structure domains: Biosynthetic peptidoglycan transglycosylase-like
