Function and Biology Details
Reaction catalysed:
Preferential cleavage: Ala-|-, Val-|- in bacterial cell walls, elastin and other proteins.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Alpha-lytic protease (preferred)
PDBe Complex ID:
PDB-CPX-133494 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alpha-lytic protease
Molecule details ›
Chains: A, B
Length: 198 amino acids
Theoretical weight: 19.82 KDa
Source organism: Lysobacter enzymogenes
Expression system: Escherichia coli
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 198 amino acids
Theoretical weight: 19.82 KDa
Source organism: Lysobacter enzymogenes
Expression system: Escherichia coli
UniProt:
- Canonical:
P00778 (Residues: 200-397; Coverage: 53%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Alpha-lytic protease
Molecule details ›
Chains: C, D
Length: 166 amino acids
Theoretical weight: 17.84 KDa
Source organism: Lysobacter enzymogenes
Expression system: Escherichia coli
UniProt:
Sequence domains: Alpha-lytic protease prodomain
Structure domains: GMP Synthetase; Chain A, domain 3
Length: 166 amino acids
Theoretical weight: 17.84 KDa
Source organism: Lysobacter enzymogenes
Expression system: Escherichia coli
UniProt:
- Canonical: P00778 (Residues: 34-199; Coverage: 45%)
Sequence domains: Alpha-lytic protease prodomain
Structure domains: GMP Synthetase; Chain A, domain 3
