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
- Clp ATPase, C-terminal
- P-loop containing nucleoside triphosphate hydrolase
- ClpP, histidine active site
- ClpP, Ser active site
- ClpP/crotonase-like domain superfamily
- ATPase, AAA-type, core
4 more domains
Structure analysis Details
Assembly composition:
hetero 28-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141327 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent Clp protease proteolytic subunit
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 192 amino acids
Theoretical weight: 21.52 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: Clp protease
Length: 192 amino acids
Theoretical weight: 21.52 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P0A6G7 (Residues: 16-207; Coverage: 93%)
Sequence domains: Clp protease
ATP-dependent Clp protease ATP-binding subunit ClpX
Molecule details ›
