Caseinolytic peptidase P (ClpP)

ClpP (caseinolytic peptidase P) is a highly conserved serine protease found in bacteria, mitochondria of eukaryotic cells, and chloroplasts. In mammalian cells, it is localized to the mitochondrial matrix and forms part of the ATP-dependent ClpXP proteolytic complex. Its primary function is to maintain protein homeostasis by degrading misfolded or damaged proteins within mitochondria. It assembles into a tetradecameric complex composed of two stacked heptameric rings, creating a barrel-shaped structure. The active site contains a Ser-His-Asp catalytic triad. Degradation of larger proteins requires association with an ATP-dependent chaperone such as ClpX. Upregulation has been observed in various human tumors. Both activators and inhibitors targeting this enzyme can disrupt oxidative phosphorylation in cancer cells—inducing apoptosis—making it a potential therapeutic target for cancer treatment as well as bacterial infections.

Disruption of oxidative phosphorylation, induction of apoptosis