Function and Biology Details
Reaction catalysed:
Preferential cleavage of bonds with hydrophobic residues in P1'.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Serralysin-like metalloprotease, C-terminal
- Hemolysin-type calcium-binding conserved site
- RTX calcium-binding nonapeptide repeat
- Peptidase M10 serralysin, C-terminal
- Peptidase M10, metallopeptidase
- Serralysin-like metallopeptidase domain
- Peptidase, metallopeptidase
- Metallopeptidase, catalytic domain superfamily
1 more domain
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Serralysin C and peptide (preferred)
PDBe Complex ID:
PDB-CPX-147684 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serralysin C
Molecule details ›
Chain: P
Length: 462 amino acids
Theoretical weight: 49.71 KDa
Source organism: Dickeya chrysanthemi
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 462 amino acids
Theoretical weight: 49.71 KDa
Source organism: Dickeya chrysanthemi
Expression system: Escherichia coli
UniProt:
- Canonical:
P16317 (Residues: 18-479; Coverage: 97%)
Sequence domains:
Structure domains:
