ATP-dependent Clp protease ATP-binding subunit ClpX (ClpX)

ClpX is an AAA+ ATPase protein and acts as a molecular chaperone and substrate specificity component of the ATP-dependent ClpXP protease system in Helicobacter pylori[2][5][6]. It partners with the serine protease ClpP to recognize, unfold, and translocate misfolded, damaged, or regulatory proteins into the proteolytic chamber of ClpP for degradation via ATP hydrolysis. ClpX has inherent ATPase and chaperone activities even in the absence of ClpP, functioning in bacterial stress responses and protein quality control[1][5]. ClpX and its associated Clp protease system are crucial for bacterial survival, pathogenicity, and adaptation, representing a promising antibacterial drug target although no clinically approved drugs are currently known to inhibit H. pylori ClpX directly[4]. The dysfunction of ClpX impairs H. pylori's ability to manage protein stress and express virulence factors, making it a focus of research in infection control.

Other names

ClpX proteaseClpX chaperoneHeat shock protein 100 chaperone (Hsp100 family)Helicobacter pylori ClpX

ATP-dependent protein unfolding Substrate recognition and translocation into ClpP for proteolysis[2][3][5][6] Chaperone-mediated prevention of protein aggregation under stress