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:
Sequence domains:
- ATP-dependent Clp protease proteolytic subunit
- Clp protease proteolytic subunit /Translocation-enhancing protein TepA
- ClpA/B family
- P-loop containing nucleoside triphosphate hydrolase
- ClpP, histidine active site
- ClpP, Ser active site
- ClpP/crotonase-like domain superfamily
- Clp ATPase, C-terminal
5 more domains
Structure analysis Details
Assembly composition:
hetero 22-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141330 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
ATP-dependent Clp protease ATP-binding subunit ClpA
Molecule details ›
ATP-dependent Clp protease proteolytic subunit
Molecule details ›
Chains: G, H, I, J, K, L, M, N, O, P, Q, R, S, T
Length: 192 amino acids
Theoretical weight: 21.47 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Clp protease
Length: 192 amino acids
Theoretical weight: 21.47 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P0A6G7 (Residues: 15-206; Coverage: 93%)
Sequence domains: Clp protease
