Function and Biology Details
Reaction catalysed:
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137236 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Internal virion protein gp15
Molecule details ›
Chains: A, C, E, H, I, K
Length: 747 amino acids
Theoretical weight: 84.45 KDa
Source organism: Escherichia phage T7
Expression system: Escherichia coli
UniProt:
Length: 747 amino acids
Theoretical weight: 84.45 KDa
Source organism: Escherichia phage T7
Expression system: Escherichia coli
UniProt:
- Canonical:
P03725 (Residues: 1-747; Coverage: 100%)
Peptidoglycan transglycosylase gp16
Molecule details ›
Chains: B, D, F, G, J, L
Length: 1318 amino acids
Theoretical weight: 144.03 KDa
Source organism: Escherichia phage T7
Expression system: Escherichia coli
UniProt:
Sequence domains: Transglycosylase SLT domain
Length: 1318 amino acids
Theoretical weight: 144.03 KDa
Source organism: Escherichia phage T7
Expression system: Escherichia coli
UniProt:
- Canonical: P03726 (Residues: 1-1318; Coverage: 100%)
Sequence domains: Transglycosylase SLT domain
