Function and Biology Details
Reaction catalysed:
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero tetradecamer (preferred)
Assembly name:
ATP-dependent Clp protease proteolytic (preferred)
PDBe Complex ID:
PDB-CPX-161942 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent Clp protease proteolytic subunit 2
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 200 amino acids
Theoretical weight: 21.89 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Clp protease
Length: 200 amino acids
Theoretical weight: 21.89 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P9WPC3 (Residues: 16-214; Coverage: 93%)
Sequence domains: Clp protease
ATP-dependent Clp protease proteolytic subunit 1
Molecule details ›
Chains: H, I, J, K, L, M, N
Length: 194 amino acids
Theoretical weight: 21.07 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Clp protease
Length: 194 amino acids
Theoretical weight: 21.07 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P9WPC5 (Residues: 7-200; Coverage: 97%)
Sequence domains: Clp protease
