Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity (By similarity). Plays a major role in the degradation of misfolded proteins (By similarity). Required for degradation of response regulator CtrA, thus contributing to the G1-to-S transition (PubMed:9755166). Required to degrade DNA replication inhibitor toxin SocB, this function is probably the reason why the protease is essential in this organism (PubMed:24239291). 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). 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. Essential, it cannot be deleted (PubMed:9755166, PubMed:24239291). When depleted for ClpP cells arrest before the initiation of chromosome replication and are blocked in the cell division process (PubMed:9755166). Deletion of socB permits slower than wild-type growth of the clpP disruption. Belongs to the peptidase S14 family. Extended N-terminus. Extended N-terminus.