Function and Biology Details
Reactions catalysed:
Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)(2))Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein, the rest of the oligosaccharide is released intact.
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Bifunctional autolysin (preferred)
PDBe Complex ID:
PDB-CPX-128494 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional autolysin
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 36.65 KDa
Source organism: Staphylococcus epidermidis
Expression system: Escherichia coli
UniProt:
Sequence domains: GW (Gly-Tryp) dipeptide domain
Structure domains: SH3 type barrels.
Length: 334 amino acids
Theoretical weight: 36.65 KDa
Source organism: Staphylococcus epidermidis
Expression system: Escherichia coli
UniProt:
- Canonical:
O33635 (Residues: 516-847; Coverage: 25%)
Sequence domains: GW (Gly-Tryp) dipeptide domain
Structure domains: SH3 type barrels.
