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Target intelligence / Profile preview
UATP-dependent Clp protease ATP-binding subunit ClpX (ClpX)
- Target
- ClpX
- Molecular classification
- Enzyme, Hsp100/Clp family, ATP-dependent protease, Molecular chaperone
01
Overview
ClpX is an ATP-dependent molecular chaperone and a regulatory subunit of the ClpXP protease complex in Helicobacter pylori. It belongs to the heat shock protein 100 (Hsp100) family and plays a crucial role in intracellular protein remodeling, degradation, and stress response. The enzyme uses energy from ATP hydrolysis to recognize, unfold, and translocate specific substrate proteins into the proteolytic core formed by ClpP for degradation. It is essential for bacterial survival under stress conditions due to its role in protein quality control and may contribute to virulence mechanisms.
- Other names
- ATP-dependent Clp protease ATP-binding subunit ClpX (Helicobacter pylori)clpX
02
Mechanism of action
ATP hydrolysis-dependent protein unfolding and translocation for degradation by ClpP
03
Biological functions
Protein remodelingProtein degradationStress responseProtein unfoldingProtein translocationChaperone activityProtein quality control
04
Disease associations
InfectionPathogenesisVirulencePersistence within gastric mucosaResistance against host defenses
05
Safety considerations
Inhibition could potentially disrupt essential bacterial protein homeostasis and stress response.
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