3.4.21.92	malfunction	a point mutation from G to A at nucleotide 2317 of ClpC1 on chromosome V of Arabidopsis is responsible for the irm1 phenotype (typical Fe-deficiency chlorosis)	717092	
3.4.21.92	malfunction	both FlhD and FlhC regulator proteins accumulate markedly following ClpXP depletion, and their half-lives are significantly longer in the mutant cells	718089	
3.4.21.92	malfunction	ClpP1 is essential for viability. The gene can only be deleted from the chromosome when a second functional copy is provided. Over-expression of clpP1 has no effect on growth in aerobic culture or viability under anaerobic conditions or during nutrient starvation	717738	
3.4.21.92	malfunction	clpP2 over-expression is toxic	717738	
3.4.21.92	malfunction	deletion of clpX and clpP suppresses temperature-sensitive filamentation of cells carrying the ftsZ84 allele and reduces FtsZ84 degradation, consistent with ClpXP (two-component protease composed of ClpX and ClpP) playing a role in modulating the level of FtsZ (a tubulin-like protein)	717731	
3.4.21.92	malfunction	in a DELTAclpP strain, 288 genes show significant changes in relative transcript amounts as compared with the parent. Similarly, 242 genes are differentially expressed by a DELTAclpX strain. Several genes associated with cell growth are down-regulated in both mutants, consistent with the slow-growth phenotype of the DELTAclp strains. Among the up-regulated genes are those encoding enzymes required for the biosynthesis of intracellular polysaccharides and malolactic fermentation. Expression of several genes known or predicted to be involved in competence and mutacin production are down-regulated in the DELTAclp strains	718088	
3.4.21.92	malfunction	in a division-defective strain, DELTAminC, the additional deletion of clpX or clpP delays cell division and exacerbates filamentation	717731	
3.4.21.92	metabolism	presence of ATP favours assembly and ADP dissociation of the hexameric assembly. Subunit exchange kinetics is at least one order of magnitude slower than the ATP hydrolysis rate, and ClpB dynamics and activity are related processe. DnaK and substrate proteins regulate the ATPase activity and dynamics of ClpB	-, 752706	
3.4.21.92	physiological function	a mutant strain lacking the N-terminal domain of ClpX is not viable	732530	
3.4.21.92	physiological function	accessory proteins ClpT1 and ClpT2 regulate the assembly of the Clp proteolytic core in vascular plants	718212	
3.4.21.92	physiological function	adaptor protein MecA specifically interacts with both central competence regulator sigmax and protease ClpC, suggesting the formation of a ternary sigmaX-MecA-ClpC complex. MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner. A short sequence of 18 amino acids in the N-terminal domain of sigmaX is essential for the interaction with MecA and subsequent sigmaX degradation. Increased transformability of a MecA-deficient strain in the presence of subinducing SigX-inducing peptide concentrations suggests that the MecA-ClpCP proteolytic complex acts as an additional locking device to prevent competence under inappropriate conditions	-, 732009	
3.4.21.92	physiological function	arginine-phosphate and arginine-phosphorylated proteins bind to subunit ClpC1 N-terminal domain and induce millisecond dynamics. These dynamics are caused by conformational changes and do not result from unfolding or oligomerization of this domain	754176	
3.4.21.92	physiological function	Azotobacter vinelandii carries a duplicated copy of the ATPase component of the ubiquitous ClpXP protease (ClpX2), which is induced under nitrogen fixing conditions. Inactivation of clpX2 results in the accumulation of NifB and NifEN and a defect in diazotrophic growth, especially when iron is in short supply	718131	
3.4.21.92	physiological function	both protein and small-molecule activators of ClpP allosterically control the ClpP barrel conformation. Acyldepsipeptides in addition to opening the axial pore directly stimulate ClpP activity through cooperative binding. ClpP activation thus reaches beyond active site accessibility and also involves conformational control of the catalytic residues. Substoichiometric amounts of acyldepsipeptide potently prevent binding of ClpX to ClpP and, at the same time, partially inhibit ClpP through conformational perturbance. The hydrophobic binding pocket is a major conformational regulatory site with implications for both ClpXP proteolysis and acyldepsipeptide -based anti-bacterial activity	-, 732563	
3.4.21.92	physiological function	Clp chaperones ClpX and ClpC1 require the intact interaction face of subunit ClpP2 to support degradation. Binding results in an asymmetric complex where chaperones only bind to the ClpP2 side of the proteolytic core	755086	
3.4.21.92	physiological function	ClpC1 is involved in Fe homeostasis in leaves	717092	
3.4.21.92	physiological function	ClpC1-catalyzed unfolding of an SsrA-tagged protein is negatively impacted by association with the ClpS adaptor protein. ClpS-dependent inhibition of ClpC1-catalyzed SsrA-dependent protein unfolding does not require the ClpC1 N-terminal domain but instead requires the presence of an interaction surface located in the ClpC1 middle domain	-, 753915	
3.4.21.92	physiological function	ClpP enhances the unfolding activity of ClpX	717472	
3.4.21.92	physiological function	ClpXP positively regulates T3SS through RpoS degradation. In addition to the regulation of T3SS, ClpXP protease, RssB, and RpoS play a role in pectinolytic enzyme production and virulence of Dickeya dadantii	718140	
3.4.21.92	physiological function	ClpXP protease consists of the ClpX hexamer and the ClpP peptidase. Small-molecule acyldepsipeptides such as ADEP-2B compete with the IGF loops of ClpX for ClpP-cleft binding and cause exceptionally rapid dissociation of otherwise stable ClpXP complexes, suggesting that the IGF-loop interactions with ClpP must be highly dynamic	752357	
3.4.21.92	physiological function	ClpXP protease of Escherichia coli consists of the AAA+ ClpX unfoldase and the associated ClpP compartmental peptidase. Once the substrate is unfolded, ClpX translocates the unfolded polypeptide into the degradation chamber of ClpP in steps of five to eight amino acids per power stroke	717999	
3.4.21.92	physiological function	ClpXP protease tightly regulates the flagellar expression by degrading the FlhD/FlhC master regulator in EHEC. The flagellar regulon in EHEC might be controlled by ClpXP protease through two pathways, namely post-translational control of the FlhD/FlhC master regulator by degrading them and transcriptional control of the flhDC operon through the locus of enterocyte effacement (LEE)-encoded GrlR-GrlA regulatory system	718089	
3.4.21.92	physiological function	deletion of the clpP gene results in a mutant strain displaying reduced growth at high temperatures and under several other stress conditions. The mutant exhibits an increased ability to take up iron in vitro compared to the wild-type strain and displays rough and irregular surfaces and increased cell volume relative to the wild-type strain. The mutant shows decreased biofilm formation. The expression of 16 genes is changed by the deletion of the clpP gene	732717	
3.4.21.92	physiological function	highly specific association between HSP100 chaperone ClpC and the ClpP3/R core. Two conserved sequences in the N-terminus of ClpR and one in the N-terminus of ClpP3 are crucial for the ClpC-ClpP3/R sdubunit association. These N-terminal domains also influence the stability of the ClpP3/R core complex itself. A unique C-terminal sequence just downstream of the P-loop region previously in ClpC confers specificity for the ClpP3/R core and prevents association with Escherichia coli ClpP	-, 731272	
3.4.21.92	physiological function	plants defective in the chloroplast caseinolytic protease Clp system are specifically impaired in copper transporter PAA2/HMA8 protein turnover on media containing elevated copper concentrations	-, 754914	
3.4.21.92	physiological function	proteins phosphorylated on arginine residues are selectively targeted to ClpC-ClpP. Arginine phosphorylation by the McsB kinase is required and sufficient for the degradation of substrate proteins. The ClpCP protease complex alone is not active. The docking site for phosphoarginine is located in the amino-terminal domain of the ClpC ATPase	-, 754888	
3.4.21.92	physiological function	proteolysis of the LexA N-terminal domain is dependent on ClpP. In the absence of the proteolytic subunit ClpP, or one or both of the Clp ATPases, ClpX and ClpC, the LexA domains are stabilized after autocleavage	718090	
3.4.21.92	physiological function	purified ClpXP added to a cell-free transcription-translation system that uses Escherichia coli S30 cell extract, has very low proteolytic activity. Addition of exogenous ATP and an energy regeneration system improves activity	755502	
3.4.21.92	physiological function	reducing the levels of mitochondrial ClpP or ClpX renders human cancer cells more sensitive to cisplatin. Overexpression of ClpP desensitizes cells to cisplatin. Cisplatin resistance correlates with decreased cellular accumulation of cisplatin and decreased levels of diguanosine-cisplatin adducts in both mitochondrial and genomic DNA. Higher levels of cisplatin-DNA adducts are found in cells in which ClpP has been depleted. Changes in the levels of ClpP have no effect on the levels of copper transporter CTR1. The levels of copper efflux pumps ATP7A and ATP7B are increased when ClpPwas overexpressed	752813