Function and Biology Details
Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I16, Streptomyces subtilisin-type inhibitor
- Peptidase S8, subtilisin-related
- Subtilisin inhibitor-like superfamily
- Subtilisin inhibitor
- Peptidase S8, subtilisin, Ser-active site
- Peptidase S8, subtilisin, His-active site
- Peptidase S8, subtilisin, Asp-active site
- Subtilisin Carlsberg-like catalytic domain
2 more domains
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190298 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase S8/S53 domain-containing protein
Molecule details ›
Chains: A, C
Length: 274 amino acids
Theoretical weight: 27.31 KDa
Source organism: Bacillus licheniformis
UniProt:
Structure domains: Peptidase S8/S53 domain
Length: 274 amino acids
Theoretical weight: 27.31 KDa
Source organism: Bacillus licheniformis
UniProt:
- Canonical:
Q9FDF2 (Residues: 37-310; Coverage: 88%)
Structure domains: Peptidase S8/S53 domain
Subtilisin inhibitor domain-containing protein
Molecule details ›
Chains: B, D
Length: 114 amino acids
Theoretical weight: 11.92 KDa
Source organism: Streptomyces caespitosus
Expression system: Escherichia coli
UniProt:
Sequence domains: Subtilisin inhibitor-like
Structure domains: Subtilisin inhibitor-like
Length: 114 amino acids
Theoretical weight: 11.92 KDa
Source organism: Streptomyces caespitosus
Expression system: Escherichia coli
UniProt:
- Canonical: Q9FDS0 (Residues: 29-141; Coverage: 97%)
Sequence domains: Subtilisin inhibitor-like
Structure domains: Subtilisin inhibitor-like
