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:
- not assigned
Sequence domains:
- Peptidase S8, subtilisin-related
- Peptidase S8/S53 domain superfamily
- Peptidase S8 propeptide/proteinase inhibitor I9
- Peptidase S8 propeptide/proteinase inhibitor I9 superfamily
- Peptidase S8, subtilisin, His-active site
- Peptidase S8, subtilisin, Asp-active site
- Subtilisin Carlsberg-like catalytic domain
- Peptidase S8/S53 domain
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Subtilisin E (preferred)
PDBe Complex ID:
PDB-CPX-137497 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Subtilisin E
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 27.75 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Length: 275 amino acids
Theoretical weight: 27.75 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
- Canonical:
P04189 (Residues: 107-381; Coverage: 78%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Subtilisin E
Molecule details ›
Chain: B
Length: 71 amino acids
Theoretical weight: 7.98 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
Sequence domains: Peptidase inhibitor I9
Structure domains: Peptidase S8 propeptide/proteinase inhibitor I9
Length: 71 amino acids
Theoretical weight: 7.98 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
- Canonical: P04189 (Residues: 36-106; Coverage: 20%)
Sequence domains: Peptidase inhibitor I9
Structure domains: Peptidase S8 propeptide/proteinase inhibitor I9
