We examined the binding site of c-di-GMP with ClpP and demonstrated that c-di-GMP enhances the peptidase activity of ClpP. Furthermore, ClpP is shown to play a vital regulatory role in bacterial motility and can activate bacterial motility in the presence of high c-di-GMP level. This ...
and EGY1 proteases (Adam et al.2006; Zheng et al.2006). The ATP-dependent Clp peptidase has been studied, and the plastid Clp proteolytic system in plants consists of five ClpP proteins, four ClpR proteins, and three Clp chaperones (ClpC1, ClpC2, and ClpD; Constan ...
tameric rings of ClpP. One or both sides of the peptidase core is flanked by a single homologous hexameric Clp chaperone complex. The Clp chaperone complex is formed by the Hsp100 chaperone protein ClpX or ClpA, which harbor one or two AAA+ domains, respectively (Wang et al., 1997; Yu...
ClpPStenotrophomonas maltophiliaPeptidaseBacterial motilityCyclic di-GMP (c-di-GMP) is a crucial secondary messenger in bacterial cells, profoundly impacting various physiological and biochemical processes. Numerous studies showed that c-di-GMP regulates specific bacterial pathways by interacting with related ...
Caseinolytic protease P (ClpP) is a tetradecameric peptidase which assembles with chaperones such as ClpX to gain proteolytic activity. Acyldepsipeptides (ADEPs) represent small molecule mimics of ClpX, which bind into hydrophobic pockets on the apical site of the complex and thereby induce ...
C-di-GMP ClpP Stenotrophomonas maltophilia Peptidase Bacterial motility 1. Introduction Stenotrophomonas maltophilia is the third most prevalent non-fermentative bacterium isolated in clinical settings, surpassed only by Pseudomonas aeruginosa and Acinetobacter species. This organism is classified as a Gram-neg...
The mitochondrial protease complex (ClpXP), which consists of caseinolytic mitochondrial matrix peptidase X (ClpX) and caseinolytic protease P (ClpP) and mediates the degradation of misfolded, damaged, and oxidized proteins, is essential for maintaining mitochondrial homeostasis. ClpXP has been ...
Clp proteins belong to the AAA+ (ATPases associated with diverse cellular activities) superfamily, and function as a complex of two components, namely the peptidase subunit (ClpP) and the regulatory subunits (ATPases) [9,10,13,14]. ClpK is amongst the recently identified ATPases. Other AT...