Structure-function analysis of the bacterial ClpE/ClpP AAA+ protease

General and regulatory proteolysis in bacteria is executed by a set of ATP-dependent proteases composed of hexameric ring-forming AAA+ proteins and associated peptidase barrels (e.g. ClpP). These AAA+ proteases play crucial roles in stress protection and bacterial virulence. Here, we provide the first biochemical characterization of the potential drug target ClpE/ClpP from Enterococcus faecalis. We show that ClpE/ClpP forms an autonomous and efficient protease, which degrades misfolded and aggre