CATH Classification

Domain Context

CATH Clusters

Superfamily 2-enoyl-CoA Hydratase; Chain A, domain 1
Functional Family ATP-dependent Clp protease proteolytic subunit

Enzyme Information

3.4.21.92
Endopeptidase Clp.
based on mapping to UniProt P63788
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).
-!- Belongs to peptidase family S14.

UniProtKB Entries (1)

P63788
CLPP_STRR6
Streptococcus pneumoniae R6
ATP-dependent Clp protease proteolytic subunit

PDB Structure

PDB 1Y7O
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.
Gribun, A., Kimber, M.S., Ching, R., Sprangers, R., Fiebig, K.M., Houry, W.A.
J.Biol.Chem.