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:
homo heptamer (preferred)
Assembly name:
ATP-dependent Clp protease proteolytic subunit (preferred)
PDBe Complex ID:
PDB-CPX-160374 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease proteolytic subunit
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 199 amino acids
Theoretical weight: 22.04 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1
Length: 199 amino acids
Theoretical weight: 22.04 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P80244 (Residues: 2-197; Coverage: 100%)
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup:
P21212
Expression system: Escherichia coli BL21(DE3)
