Function and Biology Details
Reaction catalysed:
Hydrolyzes proteins with a preference for Tyr or Phe in the P1' position. Has no action on amino-acid p-nitroanilides.
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157466 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Extracellular small neutral protease
Molecule details ›
Chains: A, C, E, G, I, K
Length: 134 amino acids
Theoretical weight: 14.57 KDa
Source organism: Streptomyces caespitosus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Streptomyces extracellular neutral proteinase (M7) family
Structure domains: Collagenase (Catalytic Domain)
Length: 134 amino acids
Theoretical weight: 14.57 KDa
Source organism: Streptomyces caespitosus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P56406 (Residues: 2-132; Coverage: 99%)
Sequence domains: Streptomyces extracellular neutral proteinase (M7) family
Structure domains: Collagenase (Catalytic Domain)
Subtilisin inhibitor domain-containing protein
Molecule details ›
Chains: B, D, F, H, J, L
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
