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:
monomeric (preferred)
Assembly name:
Membrane-bound lytic murein transglycosylase F (preferred)
PDBe Complex ID:
PDB-CPX-191114 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Membrane-bound lytic murein transglycosylase F
Molecule details ›
Chain: A
Length: 435 amino acids
Theoretical weight: 49.1 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains: Periplasmic binding protein-like II
Length: 435 amino acids
Theoretical weight: 49.1 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q9HXN1 (Residues: 28-460; Coverage: 93%)
Sequence domains:
Structure domains: Periplasmic binding protein-like II
