FEATURES

FAMILY

DESCRIPTION

Also known as CLPP_BACSU, clpP, yvdN. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX (PubMed:20305655). Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor (PubMed:16899079). Probably the major protease that degrades proteins tagged by trans-translation (PubMed:11395451, PubMed:31155236). Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes (PubMed:20305655, PubMed:22080375). Forms large heterooligomeric complexes consisting of an ATPase component (ClpX, ClpC or ClpE) and a proteolytic component (ClpP)(PubMed:20305655).

EXTERNAL LINKS

clpP

ATP-dependent Clp protease proteolytic subunit

clpP

Molecular Synopsis