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). 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). Low intrinsic peptidase activity is stimulated by ATP-binding subunits ClpC, ClpE and ClpX. Activity is disregulated by acyldepsipeptides (ADEP) antibiotics, which negate the need for ATP-binding subunits for activation and which makes it into an unregulated protease. Each ClpP subunit binds 1 ADEP molecule, which prevents binding of ClpX. ADEP binding causes conformational shifts that open the gated pore of the ring (PubMed:20305655). Protease activity is inhibited by diisopropylfluoro-phosphate (PubMed:22080375). Protease activity is inhibited by bortezomib, an oncology drug originally designed to work on the human proteasome (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). By heat shock, salt stress, ethanol stress, oxidative stress, glucose limitation and oxygen limitation. Peptide exit pores open in the compressed state; in this conformation the active site residues move apart and the protease cannot be active. No degradation of trans-translationally tagged-peptides (PubMed:11395451, PubMed:31155236). Triple rqcH clpP ssrA mutants cannot be generated (ssrA, or tmRNA, encodes the SsrA tag added to nascent proteins in stalled ribosomes by trans-translation, targeting the nascent protein for degradation) (PubMed:31155236). Belongs to the peptidase S14 family.