In the important human pathogen, Streptococcus pneumoniae, the ClpP protease is essential for modulating virulence and the cellular stress response. Here, the Clp ATPase chaperones associate with the ClpP protease to mediate general and targeted proteolysis. To identify the ClpP-dependent function of the Clp ATPases, we modified the IGF-tripeptide ClpP recognition motif for each of the Clp ATPases. We assess the ClpP-dependent phenotypes associated with inactivation of each of the ClpEP (XCP), ClpCP (XEP) and ClpXP (CEP) proteases compared to the wild type (XCEP).