ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes (By similarity). Forms a complex with ClpP1 and ClpP2. Interacts with RseA but does not seem to help degrade it. Belongs to the ClpX chaperone family.