3.4.21.92	A153C	the structure of a crosslinked Escherichia coli ClpP are determined in which the two heptameric rings of ClpP are held together by disulfide bonds. While all Escherichia coli ClpP structures solved to date are in the extended state, the crosslinked ClpP structure is found to be in the compact state. Under reducing condition Km (N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin) is similar to wild-type but kcat is 32fold lower. Under non-reducing conditions mutant is inactive and does not bind its cognate chaperone	718406	
3.4.21.92	A153P	crystallization data, disruption of handle region resulting in an altered ring-ring dimerization interface	669324	
3.4.21.92	Delta1-10	deletion of the N-terminal 10, 14, or 17 residues of mature ClpP allows these mutants to degrade alpha-casein, a natively unfolded protein	717989	
3.4.21.92	DELTA1-14	deletion of the N-terminal 10, 14, or 17 residues of mature ClpP allows these mutants to degrade alpha-casein, a natively unfolded protein	717989	
3.4.21.92	DELTA1-17	deletion of the N-terminal 10, 14, or 17 residues of mature ClpP allows these mutants to degrade alpha-casein, a natively unfolded protein	717989	
3.4.21.92	E135A	mutant shows no activity	717089	
3.4.21.92	E135R	mutant shows no activity	717089	
3.4.21.92	E8A/R12A/E14A/R15A	residues 8-15 form the channel loop of the pore: when charged residues in the channel (amino acids 8-15) are changed with alanine this mutant cleaves the decapeptide at a rate 8fold faster than observed with wild-type ClpP but cleaves the dipeptide at a comparable rate. Mutant shows a substantial GFP-ssrA degradation similar to wild-type	717989	
3.4.21.92	E8G/Q9G/T10G/S11G/R12G/G13G/E14G/R15G	residues 8-15 form the channel loop of the pore: when replaced with eight glycines this mutant cleaves the decapeptide at a rate 8fold faster than observed with wild-type ClpP but cleaves the dipeptide at a comparable rate. Mutant shows a much slower degradation of GFP-ssrA	717989	
3.4.21.92	E8G/R12G/E14G/R15G	residues 8-15 form the channel loop of the pore: when charged residues in the channel (amino acids 8-15) are changed with glycine this mutant cleaves the decapeptide at a rate 8fold faster than observed with wild-type ClpP but cleaves the dipeptide at a comparable rate. Mutant shows a much slower degradation of GFP-ssrA	717989	
3.4.21.92	E8R/R12E/E14R/R15E	residues 8-15 form the channel loop of the pore: when charged residues in the channel (amino acids 8-15) are reversed this mutant cleaves the decapeptide at a rate 8fold faster than observed with wild-type ClpP but cleaves the dipeptide at a comparable rate. Mutant shows a much slower degradation of GFP-ssrA	717989	
3.4.21.92	G127	mutant shows no activity	717089	
3.4.21.92	G128	mutant shows no activity	717089	
3.4.21.92	G131	mutant shows no activity	717089	
3.4.21.92	G773R	inactive mutant	717092	
3.4.21.92	H230A	RKH mutant to investigate the role of the RKH sequence loops	683865	
3.4.21.92	I19A	mutant shows wild-type level of dipeptide cleavage, 20fold increase in decapeptide cleavage compared to wild-type, in contrast to wild-type mutant degrades 113-residue unfolded I27 domain of human titin. Mutant shows high decrease in ClpX affinity	717989	
3.4.21.92	I19D	mutant shows 16fold increase in decapeptide cleavage compared to wild-type	717989	
3.4.21.92	I19L	mutant shows 6fold increase in decapeptide cleavage compared to wild-type	717989	
3.4.21.92	K229A	RAH mutant to investigate the role of the RKH sequence loops	683865	
3.4.21.92	K25A	mutant shows wild-type level of dipeptide cleavage, 1.5fold increase in decapeptide cleavage compared to wild-type. Mutant shows only moderate decrease in ClpX affinity	717989	
3.4.21.92	L144E	mutant shows no activity	717089	
3.4.21.92	L144G	mutant shows no activity	717089	
3.4.21.92	L144M	Km (N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin): 0.523 mM, kcat: 0.003/sec	717089	
3.4.21.92	L144R	mutant shows no activity	717089	
3.4.21.92	L23A	mutant shows wild-type level of dipeptide cleavage, 5fold increase in decapeptide cleavage compared to wild-type. Mutant shows only moderate decrease in ClpX affinity	717989	
3.4.21.92	L24A	mutant shows wild-type level of dipeptide cleavage, 20fold increase in decapeptide cleavage compared to wild-type. Mutant shows high decrease in ClpX affinity	717989	
3.4.21.92	additional information	a clpC knockout strain expressing ComGA-GFP fails to exhibit delocalization. Polar accumulation of McsB-YFP is more intense in a clpC knockout	700285	
3.4.21.92	additional information	antisense clpR4 repression lines with up to 90% loss of wild-type enzyme level, phenotype results in slow growth and leaf variegation. Chlorosis is most severe in younger leaves, exhibiting impaired chloroplast development and mesophyll cell differentiation	670633	
3.4.21.92	additional information	enzyme complex ClpPRS consists of five ClpP protease molecules, four nonproteolytic ClpR molecules, and two associated ClpS molecules. Introduction of ClpR2 insertion mutant results in reduced accumulation of complex, leading to pale-green phenotype with delayed shoot development, smaller chloroplasts, decreased thylakoid accumulation, and increased plastoglobule accumulation	670535	
3.4.21.92	additional information	enzyme deletion mutant, markedly diminished global protein degradation, bulk protein is rendered prone to aggregation	669088	
3.4.21.92	additional information	in the absence of ClpA, deletion of the ClpP N-terminus increases the initial degradation rate of large peptide substrates 5-15fold. ClpPDELTAN accelerates degradation of insulin chain B and induces distinct rapid and slow phases of product formation. The distinct slow phase of product formation is eliminated by the addition of hydroxylamine, truncation of the N-terminus leads to stabilization of the acyl-enzyme intermediate	696224	
3.4.21.92	additional information	in the clpP mutant (strain SG22159), no degradation of the alkaline phosphatase-aggregate takes place	696989	
3.4.21.92	additional information	isoform ClpP1 inactivation mutant, little or no net degradation of chlorophyll under conditions that drive chlorophyll degradation in wild-type. Isoform ClpP2 inactivation mutant, chlorophyll degradation is similar to wild-type	667341	
3.4.21.92	additional information	labeling with 13Cmethyl-methanethiosulfonate (13C-MMTS) at the N-termini of the subunits comprising the Escherichia coli ClpP protease that reveals multiple conformations of gating residues in this complex. These N-terminal residues adopt a single conformation upon gate opening	717708	
3.4.21.92	additional information	mutant overexpressing chlorophyllide a oxygenase are mutagenized by incubation in ethylmethane sulfonate. One mutant has a defect in the ClpC1 subunit of the Clp protease	676527	
3.4.21.92	additional information	RKH loops are important for in substrate recognition	683865	
3.4.21.92	additional information	spontaneously generated mutants resistant to rufomycin I involve seven unique single nucleotide polymorphism mutations at three distinct codons within the N-terminal domain of clpC1 (V13, H77, and F80)	-, 752509	
3.4.21.92	additional information	transcription of luxR(mA) is significantly repressed in the clpP mutant, and introduction of luxR(mA) restored, in part, massetolide biosynthesis and swarming motility of the clpP mutant. Addition of casamino acids enhances the transcription of luxR(mA) and massABC in the clpP mutant, leading to a partial rescue of massetolide production and swarming motility	-, 698609	
3.4.21.92	R228A	AKH mutant to investigate the role of the RKH sequence loops	683865	
3.4.21.92	R22A	mutant shows wild-type level of dipeptide cleavage, 1.5fold increase in decapeptide cleavage compared to wild-type. Mutant shows high decrease in ClpX affinity	717989	
3.4.21.92	S101A	mutation of the active site Ser-101 in ClpP3 inactivates the entire ClpCP3/R protease, the mutation has no effect on the formation of the recombinant ClpP3/R core complex of 270 kDa. The mutated ClpP3/R complex stimulates the steady-state ATPase activity of ClpC to the same extent as wild-type ClpP3/R. The mutated ClpP3/R core fails to degrade the alpha-casein nor the more sensitive FITC-casein	698890	
3.4.21.92	S21A	mutant shows wild-type level of dipeptide cleavage, 5fold increase in decapeptide cleavage compared to wild-type. Mutant shows high decrease in ClpX affinity	717989	
3.4.21.92	S499C	mutation introduced for FRET measurements. Labelling of S499C with fluorescent probes induces a 10-20fold increase in both chaperone and ATPase activities	-, 752706	
3.4.21.92	S61A/Y63V/L83A/Y91V	mutations in hydrophobic patch of subunit ClpP1. Complex formation and processing still occurs. The complex containing the mutant is catalytically active	755086	
3.4.21.92	S97A	inactive. Overexpression has no effect on sensitivity of cells to cisplatin	752813	
3.4.21.92	S98A	inactive trapping variant	-, 754888	
3.4.21.92	S98A	mutant shows no activity	717089	
3.4.21.92	S99A	does not digest peptide into smaller fragments	699539	
3.4.21.92	Y20A	mutant shows wild-type level of dipeptide cleavage, 5fold increase in decapeptide cleavage compared to wild-type. Mutant shows high decrease in ClpX affinity	717989	
3.4.21.92	Y63A	gain-of-function mutant, inhibits staphylococcal growth. The mutant becomes an uncontrolled protease that actively hydrolyzes cell division protein FtsZ in vitro. Expression of mutant phenocopies treatment with acyldepsipeptides, inhibition of cell division occurs as does showing sterilizing with rifampicin antibiotics	-, 752359	
3.4.21.92	Y75V/Y95V	mutations in hydrophobic patch of subunit ClpP2.Complex formation and processing still occurs. The complex containing the mutant is catalytically inactive	755086