The highly conserved ClpP protease is a potential biological target against bacteria.It consists of two heptameric rings that enclose a large chamber.ClpP might undergo switching between an active extended state required for substrate degradation and an inactive compact state allowing product release.Here, we present the wild type ClpP structures in two distinct states from Staphylococcus aureus.One strucutre is closely similar to those solved ClpP structures in extended states; the other is novel, in which the handle domain kinks to take a compressed conformation.Based on structural analysis and Molecular Dynamics simulations, we propose a mechanism that the dynamic conformational change of SaClpP is mediated by electrostatic interaction and hydrogen bonding network between Arg170 and Asp169 from apposing rings.The handle domain controls the degradative products exit the chamber by dynamic conformational switching from extended state to compressed state.Our work provides critical information for understanding the dynamics of enzymatic cycle of the ClpP family proteins in general and light up the road for the future anti-bacteria drug discovery studies.