ClpHsp100

ClpHsp100 is a protein belonging to the Hsp100 family of molecular chaperones, found in the bacterium *Clostridium perfringens*. These chaperones are known for their crucial roles in protein homeostasis, assisting in protein folding, refolding of misfolded or aggregated proteins, and protein disaggregation. The Hsp100 family, also known as Clp proteins or AAA+ unfoldases, are ATP-dependent molecular machines that utilize the energy from ATP hydrolysis to exert mechanical force on protein substrates, leading to their unfolding or disassembly.

In *C. perfringens*, ClpHsp100 is implicated in the stress response and survival of the bacterium, particularly under conditions of heat shock or other environmental stresses that can lead to protein damage. Like other Hsp100 proteins, ClpHsp100 likely functions as part of a larger proteolytic complex, often in conjunction with Clp proteases. This collaboration allows for the targeted degradation of damaged proteins, thereby preventing the accumulation of toxic protein aggregates and maintaining cellular function. Research into ClpHsp100 contributes to understanding bacterial adaptation mechanisms and potential targets for antimicrobial strategies.