3.4.21.92 31-knotted methyltransferase YbeA-ssrA + H2O substrate contains a deep trefoil knot, with 70 and 34 residues lying to the N- and C-terminus of the knotted core, and is fused to the 11-amino acid ssrA degron Escherichia coli ? - ? 449299 3.4.21.92 52-knotted ubiquitin C-terminal hydrolase L1-ssrA substrate is fused to the 11-amino acid ssrA degron Escherichia coli ? - ? 449368 3.4.21.92 Abz-KASPVSLGY(NO2)D + H2O - Escherichia coli ? - ? 418371 3.4.21.92 alkaline phosphatase + H2O - Escherichia coli ? - ? 360985 3.4.21.92 alpha-casein + H2O is completely degraded by ClpC and ClpP3/R within 20 min Synechococcus elongatus ? - ? 366244 3.4.21.92 antitoxin epsilon + H2O Epsilon is an antitoxin of the Epsilon/Zeta toxin-antitoxin system family, purified Zeta toxin protects the Epsilon protein from rapid ClpXP-catalyzed degradation Bacillus subtilis ? - ? 430883 3.4.21.92 Arc-ssrA + H2O Arc repressor with a C-terminal ssrA tag Escherichia coli peptides - ? 394241 3.4.21.92 Bacteriophage lambdaO-DNA replication protein + H2O degraded by ClpXP Escherichia coli Hydrolyzed bacteriophage lambdaO-DNA replication protein - ? 15826 3.4.21.92 Bacteriophage lambdaO-DNA replication protein + H2O degraded by ClpXP Escherichia coli W3110 B178 Hydrolyzed bacteriophage lambdaO-DNA replication protein - ? 15826 3.4.21.92 beta-casein + H2O - Pisum sativum ? - ? 36618 3.4.21.92 beta-casein + H2O - Bacillus subtilis ? - ? 36618 3.4.21.92 beta-casein + H2O - Bacillus subtilis 168 ? - ? 36618 3.4.21.92 beta-Galactosidase fusion proteins + H2O - Escherichia coli Hydrolyzed beta-galactosidase fusion protein - ? 15825 3.4.21.92 casein + H2O - Bacillus subtilis ? - ? 15445 3.4.21.92 casein + H2O - Escherichia coli ? - ? 15445 3.4.21.92 casein + H2O - Escherichia coli small peptides derived from casein - ? 15817 3.4.21.92 casein + H2O alpha-casein Escherichia coli small peptides derived from casein - ? 15817 3.4.21.92 casein + H2O - Escherichia coli RGC125 (lon-) small peptides derived from casein - ? 15817 3.4.21.92 casein-fluorescein isothiocyanate + H2O - Mus musculus ? - ? 404609 3.4.21.92 central competence regulator sigmax + H2O adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner Streptococcus thermophilus ? - ? 430925 3.4.21.92 central competence regulator sigmax + H2O adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner Streptococcus thermophilus ATCC BAA-250 ? - ? 430925 3.4.21.92 chlorophyll + H2O - Synechococcus elongatus ? - ? 384442 3.4.21.92 chlorophyllide a oxygenase + H2O ClpC1 regulates the level of chlorophyllide a oxygenase, chloroplast ClpC1 regulates chlorophyll b biosynthesis Arabidopsis thaliana ? - ? 394288 3.4.21.92 CM-titin-ssrA + H2O - Escherichia coli ? - ? 394289 3.4.21.92 COMK + H2O ClpCP, MecA required Bacillus subtilis ? - ? 394290 3.4.21.92 copper transporter PAA2/HMA8 + H2O - Arabidopsis thaliana ? - ? 449774 3.4.21.92 copper transporter PAA2/HMA8 + H2O - Arabidopsis thaliana Col-0 ? - ? 449774 3.4.21.92 CtrA + H2O - Caulobacter vibrioides ? - ? 431745 3.4.21.92 elongation factor Ts + H2O clpP6 mutant have impaired photosynthesis and chloroplast development Arabidopsis thaliana ? - ? 394321 3.4.21.92 fEGFP-ssrA + H2O i.e. N-terminal His-tagged superfolder enhanced green fluorescent protein with the ssrA tag sequence at the C-terminus Escherichia coli ? - ? 449914 3.4.21.92 FITC-casein + H2O neither ClpC nor ClpP3/R alone degrade FITC-casein but they do when added together. No proteolytic activity when ClpP3 alone is combined with ClpC Synechococcus elongatus ? - ? 384720 3.4.21.92 FixK2 + H2O substrate is a CRP-like transcription factor that controls the endosymbiotic lifestyle of Bradyrhizobium japonicum. Degradation occurs by the ClpAP1 chaperone-protease complex, but not by the ClpXP1 chaperone-protease complex, and is inhibited by the ClpS1 adaptor protein. The last 12 amino acids of FixK2 are recognized by ClpA Bradyrhizobium japonicum ? - ? 430992 3.4.21.92 FlhC subunit + H2O + ATP subunit of the flagellar master transcriptional regulator complex, FlhD4C2. Flagellum-related protein FliT selectively increases ClpXP-dependent proteolysis of the FlhC subunit in the FlhD4C2 complex. FliT promotes the affinity of ClpX against FlhD4C2 complex, whereas FliT does not directly interact with ClpX. FliT interacts with the FlhC in FlhD4C2 complex and increases the presentation of the FlhC recognition region to ClpX. The DNA-bound form of FlhD4C2 complex is resistant to ClpXP proteolysis Salmonella enterica ? - ? 430994 3.4.21.92 FlhC subunit + H2O + ATP subunit of the flagellar master transcriptional regulator complex, FlhD4C2. Flagellum-related protein FliT selectively increases ClpXP-dependent proteolysis of the FlhC subunit in the FlhD4C2 complex. FliT promotes the affinity of ClpX against FlhD4C2 complex, whereas FliT does not directly interact with ClpX. FliT interacts with the FlhC in FlhD4C2 complex and increases the presentation of the FlhC recognition region to ClpX. The DNA-bound form of FlhD4C2 complex is resistant to ClpXP proteolysis Salmonella enterica ATCC 700720 ? - ? 430994 3.4.21.92 FR-GFP + H2O ClpCP3/R with ClpS1 take over 20 min to completely degrade FR-GFP, whereas the ClpAP protease degrades all FR-GFP within 2 min Synechococcus elongatus ? - ? 405190 3.4.21.92 GFP-K17 fusion protein + H2O - Bacillus subtilis ? - ? 394333 3.4.21.92 GFP-ssrA + H2O - Escherichia coli ? - ? 418677 3.4.21.92 Glucagon + H2O cleavage at multiple sites Escherichia coli Hydrolyzed glucagon - ? 15306 3.4.21.92 Glucagon + H2O cleavage at multiple sites Escherichia coli CSH100 (ClpA) Hydrolyzed glucagon - ? 15306 3.4.21.92 Gly-L-Arg-7-amido-4-methylcoumarin + H2O substrate for the recombinant ClpP Plasmodium falciparum Gly-L-Arg + 7-amino-4-methylcoumarin - ? 405298 3.4.21.92 green-fluorescent-protein-ssrA + H2O - Escherichia coli ? - ? 384838 3.4.21.92 Hsp90 + H2O - Arabidopsis thaliana ? - ? 392232 3.4.21.92 insulin chain B + H2O - Escherichia coli ? - ? 405487 3.4.21.92 LacZ + H2O - Mycobacterium tuberculosis ? proteolytic subunit ClpP2 over-expression induces degradation of untagged LacZ ? 432063 3.4.21.92 LacZ + H2O - Mycobacterium tuberculosis H37Rv ? proteolytic subunit ClpP2 over-expression induces degradation of untagged LacZ ? 432063 3.4.21.92 Lambda O Arc + H2O Arc repressor with a N-terminal lambda O degradation tag Escherichia coli ? - ? 394395 3.4.21.92 lambda O CM-titiin + H2O - Escherichia coli ? - ? 453061 3.4.21.92 Lambda O CM-titin + H2O - Escherichia coli ? - ? 394396 3.4.21.92 Leu-Tyr-Leu-Tyr-Trp + H2O cleavage occurs primarily at Leu3-Tyr4, but significant cleavage also at Tyr2-Leu3 and Leu4-Trp5 bond Escherichia coli Leu-Tyr-Leu + Tyr-Trp - ? 15824 3.4.21.92 LexA N-terminal domain + H2O - Staphylococcus aureus ? - ? 418794 3.4.21.92 luciferase-ssrA + H2O - Escherichia coli ? - ? 385102 3.4.21.92 additional information - Escherichia coli ? - ? 89 3.4.21.92 additional information role for the Clp protease in activating Mu-mediated DNA rearrangements Escherichia coli ? - ? 89 3.4.21.92 additional information ClpP subunit has peptidase activity against very short peptides, with fewer than five amino acid residues in the absence of ClpA and nucleotide Escherichia coli ? - ? 89 3.4.21.92 additional information when activated by ClpA subunit, ClpP can degrade longer polypeptides and proteins Escherichia coli ? - ? 89 3.4.21.92 additional information physiological activation of Mu-dependent DNA rearrangements requires Clp functions. Clp plays a role in monitoring the physiological status of the cell Escherichia coli ? - ? 89 3.4.21.92 additional information ClpXP appears to be involved in plasmid maintenance and in phage Mu virulence Escherichia coli ? - ? 89 3.4.21.92 additional information the high degree of similarity among the ClpA-like proteins suggests that Clp-like proteases are likely to be important participants in energy-dependent proteolysis in prokaryotic and eukaryotic cells Escherichia coli ? - ? 89 3.4.21.92 additional information selectivity of degradation by ClpP in vivo is determined by interaction of ClpP with different regulatory ATPase subunits Escherichia coli ? - ? 89 3.4.21.92 additional information ClpP is present in a wide range of prokaryotic and eukaryotic cells and is highly conserved in plant chloroplasts Escherichia coli ? - ? 89 3.4.21.92 additional information ClpP linked to many activities, including sporulation, cell competence, stress tolerance and regulation of gene expression Bacillus subtilis ? - ? 89 3.4.21.92 additional information removing of irreversibly damaged polypeptides Escherichia coli ? - ? 89 3.4.21.92 additional information enzyme complex ClpPRS consisting of five ClpP protease molecules, four nonproteolytic ClpR molecules, and two associated ClpS molecules, is central to chloroplast biogenesis, thylakoid protein homeostasis, and plant development Arabidopsis thaliana ? - ? 89 3.4.21.92 additional information enzyme is required for release of autolysin A and pneumolysin. In vivo, it is required for growth of pneumococcus in the lungs and blood in a murine model of disease Streptococcus pneumoniae ? - ? 89 3.4.21.92 additional information enzyme is required for the growth at elevated temperature and for virulence Streptococcus pneumoniae ? - ? 89 3.4.21.92 additional information stress- and starvation-induced bulk protein turnover depends virtually exclusively on enzyme, which is also essential for intracellular protein quality control Bacillus subtilis ? - ? 89 3.4.21.92 additional information ClpP affects the expression of luxR(mA), the transcriptional regulator of the massetolide biosynthesis genes massABC, thereby regulating biofilm formation and swarming motility of Pseudomonas fluorescens SS101. At the transcriptional level, ClpP-mediated regulation of massetolide biosynthesis operates independently of regulation by the GacA/GacS two-component system Pseudomonas fluorescens ? - ? 89 3.4.21.92 additional information ClpR subunit is proteolytically inactive, thus ClpR subunit does not contribute to the proteolytic activity of the ClpP3/R core. Inclusion of ClpR is not rate-limiting for the ClpCP3/R protease. ClpC is not affected by auto-degradation as is ClpA. ClpS1 alters the substrate specificity of the ClpCP3/R protease Synechococcus elongatus ? - ? 89 3.4.21.92 additional information degradation of anchor proteins by the McsA-McsB-(ClpC or ClpE)-ClpP protease in an ATP-dependent process that involves the autophosphorylation of McsB. ClpC, ClpE and ClpP contribute to delocalization Bacillus subtilis ? - ? 89 3.4.21.92 additional information mucosal immunization with ClpP antigen induces both systemic and mucosal antibodies, and in this way reduces lung colonization in an invasive pneumococcal pneumonia model and also protects mice against death in an intraperitoneal-sepsis model. Intraperitoneal immunization of BALB/c mice with recombinant ClpP protein. ClpP protein is immunogenic in healthy children and is expressed during disease based on the elevated antibody levels in infected individuals. In vitro functional anti-ClpP antibody can kill streptococcus pneumoniae by polymorphonuclear leukocytes in a complement-dependent assay Streptococcus pneumoniae TIGR4 ? - ? 89 3.4.21.92 additional information nasal immunizations with ClpP and CbpA are efficient for induction of systemic and mucosal antibodies Streptococcus pneumoniae TIGR4 ? - ? 89 3.4.21.92 additional information the ClpP N-terminus acts as a gate controlling substrate access to the active sites, binding of ClpA opens this gate, allowing substrate entry and formation of the acyl-enzyme intermediate, and closing of the N-terminal gate stimulates acyl-enzyme hydrolysis Escherichia coli ? - ? 89 3.4.21.92 additional information recombinant mature ClpP is not capable of hydrolyzing Gly-L-Arg-7-amido-4-methylcoumarin, Gly–L-Phe-7-amido-4-methylcoumarin, and benzyloxycarbonyl-L-Gln-L-Arg-L-Arg-7-amido-4-methylcoumarin. Mature ClpP protein does not cleave N-succinyl-L-leucine-L-tyrosine-7-amido-4-methylcoumarin and N-succinyl-L-isoleucine-L-isoleucine-L-tryptophan-7-amido-4-methylcoumarin Plasmodium falciparum ? - ? 89 3.4.21.92 additional information ClpP associates with ClpX or ClpA to form the AAA+ ClpXP or ClpAP proteases Escherichia coli ? - ? 89 3.4.21.92 additional information ClpP binds to AAA+ ATPase/unfoldase, ClpA or ClpX Escherichia coli ? - ? 89 3.4.21.92 additional information one ClpP recognition motif is the presence of Ala-Ala at the extreme C-terminus of substrates. Mutating the C-terminal residues of substrates flagellar regulator FlaF and IbpA to Asp-Asp eliminates recognition Caulobacter vibrioides ? - ? 89 3.4.21.92 additional information phosphate release is the force-generating step of the ATPase cycle. Protease ClpXP translocates substrate polypeptides by highly coordinated conformational changes in up to four ATPase subunits. To unfold stable substrates like GFP, ClpXP must use this maximum successive firing capacity. The dwell duration between individual bursts of translocation is constant and governed by an internal clock, regardless of the number of translocating subunits Escherichia coli ? - ? 89 3.4.21.92 additional information protease ClpXP unfolds most domains by a single pathway, with kinetics that depend on the native fold and structural stability. Subsequent translocation or pausing occurs at rates that vary with the sequence of the unfolded substrate. During translocation, ClpXP does not exhibit a sequential pattern of step sizes, supporting a fundamentally stochastic reaction, but a mechanism of enzymatic memory results in short physical steps being more probable after short steps and longer physical steps being more likely after longer steps, allowing the enzyme to run at different speeds. Two ATP-hydrolysis events can drive more than two power strokes. Solution proteolysis is many times slower than predicted from single-molecule results Escherichia coli ? - ? 89 3.4.21.92 additional information the SsrA tag directs proteins to degradation by both ClpP1 and ClpP2. The terminal three residues of the ssrA-tag sequence are LAA. A LAA-tag is sufficient to direct proteins into the degradation pathway Mycobacterium tuberculosis ? - ? 89 3.4.21.92 additional information ClpP requires association with ClpA or ClpX to unfold and thread protein substrates through the axial pore into the inner chamber where degradation occurs Bacillus subtilis ? - ? 89 3.4.21.92 additional information ClpP requires association with ClpA or ClpX to unfold and thread protein substrates through the axial pore into the inner chamber where degradation occurs Escherichia coli ? - ? 89 3.4.21.92 additional information after phosphorylation by the McsB arginine kinase, phosphoarginine-tagged proteins are targeted to the ClpCP protease. Binding of phophoarginine proteins to one of the 12 N-terminal domain binding pockets stimulates the ATPase activity of ClpC, leading to the translocation of the captured substrate into the ClpP protease cage and to protein degradation Bacillus subtilis ? - ? 89 3.4.21.92 additional information ClpXP can easily degrade a deeply 31-knotted protein and is able to degrade 52-knotted proteins. The degradation depends critically on the location of the degradation tag and the local stability near the tag Escherichia coli ? - ? 89 3.4.21.92 additional information after phosphorylation by the McsB arginine kinase, phosphoarginine-tagged proteins are targeted to the ClpCP protease. Binding of phophoarginine proteins to one of the 12 N-terminal domain binding pockets stimulates the ATPase activity of ClpC, leading to the translocation of the captured substrate into the ClpP protease cage and to protein degradation Bacillus subtilis 168 ? - ? 89 3.4.21.92 additional information the SsrA tag directs proteins to degradation by both ClpP1 and ClpP2. The terminal three residues of the ssrA-tag sequence are LAA. A LAA-tag is sufficient to direct proteins into the degradation pathway Mycobacterium tuberculosis H37Rv ? - ? 89 3.4.21.92 additional information ClpP subunit has peptidase activity against very short peptides, with fewer than five amino acid residues in the absence of ClpA and nucleotide Escherichia coli CSH100 (ClpA) ? - ? 89 3.4.21.92 additional information when activated by ClpA subunit, ClpP can degrade longer polypeptides and proteins Escherichia coli CSH100 (ClpA) ? - ? 89 3.4.21.92 additional information ClpXP appears to be involved in plasmid maintenance and in phage Mu virulence Escherichia coli CSH100 (ClpA) ? - ? 89 3.4.21.92 additional information the high degree of similarity among the ClpA-like proteins suggests that Clp-like proteases are likely to be important participants in energy-dependent proteolysis in prokaryotic and eukaryotic cells Escherichia coli CSH100 (ClpA) ? - ? 89 3.4.21.92 additional information ClpP affects the expression of luxR(mA), the transcriptional regulator of the massetolide biosynthesis genes massABC, thereby regulating biofilm formation and swarming motility of Pseudomonas fluorescens SS101. At the transcriptional level, ClpP-mediated regulation of massetolide biosynthesis operates independently of regulation by the GacA/GacS two-component system Pseudomonas fluorescens SS101 ? - ? 89 3.4.21.92 MurAA + H2O MecA not required for degradation Bacillus subtilis ? - ? 394420 3.4.21.92 Mutated repressor of Mu prophage + H2O high susceptibility to the Clp-dependent degradation Escherichia coli Hydrolyzed mutated repressor of Mu prophage - ? 15828 3.4.21.92 N-succinyl-Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O throughout the 5 min time course, ClpP readily degrades the dipeptide, whereas ClpP3/R does not. Prolonging the incubation time with ClpP3/R to 20 min does not result in any visible degradation. Addition of ClpC to the assays also fails to produce any degradation Synechococcus elongatus N-succinyl-Ile-Ile-Trp + 7-amino-4-methylcoumarin - ? 406042 3.4.21.92 N-succinyl-L-isoleucine-L-isoleucine-L-tryptophan-7-amido-4-methylcoumarin + H2O - Plasmodium falciparum ? - ? 412567 3.4.21.92 N-succinyl-Leu-Tyr 4-methylcoumarin 7-amide + H2O - Escherichia coli N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin - ? 15827 3.4.21.92 N-succinyl-Leu-Tyr 4-methylcoumarin 7-amide + H2O - Escherichia coli RGC125 (lon-) N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin - ? 15827 3.4.21.92 N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O - Escherichia coli N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin - ? 362351 3.4.21.92 N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O - Helicobacter pylori N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin - ? 362351 3.4.21.92 N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O throughout the 5 min time course, ClpP readily degrades the dipeptide, whereas ClpP3/R does not. Prolonging the incubation time with ClpP3/R to 20 min does not result in any visible degradation. Addition of ClpC to the assays also fails to produce any degradation Synechococcus elongatus N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin - ? 362351 3.4.21.92 N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O - Staphylococcus aureus ? - ? 406044 3.4.21.92 N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O initial degradation rate is the same within error for wild-type ClpP, ClpAP, and ClpPDELTAN Escherichia coli ? - ? 406044 3.4.21.92 N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O - Plasmodium falciparum ? - ? 367755 3.4.21.92 N-succinyl-Val-Lys-Met-7-amido-4-methylcoumarin + H2O throughout the 5 min time course, ClpP readily degrades the dipeptide, whereas ClpP3/R does not. Prolonging the incubation time with ClpP3/R to 20 min does not result in any visible degradation. Addition of ClpC to the assays also fails to produce any degradation Synechococcus elongatus N-succinyl-Val-Lys-Met + 7-amino-4-methylcoumarin - ? 406046 3.4.21.92 ornithine decarboxylase CC030 + H2O - Caulobacter vibrioides ? CC0360 is rapidly degraded by ClpP protease in vitro. CC0360 is exclusively degraded by the full-length ClpXP complex and not by a version of ClpX lacking the Nterminal domain ? 432279 3.4.21.92 Oxidized insulin B-chain + H2O cleavage at multiple sites Escherichia coli Hydrolyzed insulin B-chain - ? 15315 3.4.21.92 Phe-Ala-Pro-His-Met-Ala-Leu-Val-Pro-Val + H2O synthetic polypeptide that corresponds to the 10 amino acids surrounding the in vivo processing site in ClpP subunit Escherichia coli ? - ? 15820 3.4.21.92 protein RepA + H2O model substrate from bacteriophage P1 Escherichia coli ? - ? 366201 3.4.21.92 RNA Helicase + H2O - Arabidopsis thaliana ? - ? 394490 3.4.21.92 RpoS sigma factor + H2O with the assistance of recognition factor RssB, ClpXP degrades the RpoS sigma factor Dickeya dadantii ? - ? 419039 3.4.21.92 RsiW + H2O ClXCP, AA at C-terminal as degradation tag Bacillus subtilis ? - ? 394491 3.4.21.92 Sda + H2O ClpXP, VSS at C-terminal as degradation tag Bacillus subtilis ? - ? 394497 3.4.21.92 SpollAB + H2O ClpCP, LCN at C-terminal as degradation tag, MecA not required, production of ClpP is strongly increased in response to heat shock or other stress signals, ClpP removes heat damaged proteins Bacillus subtilis ? - ? 394508 3.4.21.92 Spx + H2O ClpCP, MecA or YpbH required for degradation Bacillus subtilis ? - ? 394510 3.4.21.92 Spx + H2O ClpXP, LAN at C-terminal as degradation tag, MecA not required Bacillus subtilis ? - ? 394510 3.4.21.92 SsrA tagged proteins + H2O ClpXP, AA at C-terminal as degradation tag Bacillus subtilis ? - ? 394512 3.4.21.92 ssrA-dabsyl + H2O initial rate of degradation of this intermediate-sized substrate is 3fold faster with ClpAP as compared to wild-type Clp and 5fold faster with ClpPDELTAN as compared to wild-type ClpP Escherichia coli ? - ? 406688 3.4.21.92 SsrA-tagged LacZ + H2O both proteolytic subunits ClpP1 and ClpP2 degrade SsrA-tagged LacZ Mycobacterium tuberculosis ? - ? 432383 3.4.21.92 SsrA-tagged LacZ + H2O both proteolytic subunits ClpP1 and ClpP2 degrade SsrA-tagged LacZ Mycobacterium tuberculosis H37Rv ? - ? 432383 3.4.21.92 stalk synthesis transcription factor TacA + H2O TacA degradation is controlled during the cell cycle dependent on the ClpXP regulator CpdR and stabilization of TacA increases degradation of another ClpXP substrate, CtrA, while restoring deficiencies associated with prolific CpdR activity Caulobacter vibrioides ? - ? 432384 3.4.21.92 Starvation proteins + H2O the ClpP proteolytic subunit plays a subtle but important role when cells are recovering from starvation. This enzyme is important in the selective degradation of starvation proteins when growth resumes Escherichia coli ? - ? 369543 3.4.21.92 Suc-AAPF-4-methylcoumarin-7-amide + H2O - Plasmodium falciparum ? - ? 419086 3.4.21.92 Suc-AFK-4-methylcoumarin-7-amide + H2O - Plasmodium falciparum ? - ? 419087 3.4.21.92 Suc-IA-4-methylcoumarin-7-amide + H2O - Plasmodium falciparum ? - ? 419089 3.4.21.92 Suc-IIW-4-methylcoumarin-7-amide + H2O - Plasmodium falciparum ? - ? 419090 3.4.21.92 Suc-LY-4-methylcoumarin-7-amide + H2O - Plasmodium falciparum ? - ? 419092 3.4.21.92 Succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide + H2O ClpP subunit alone Escherichia coli Succinyl-Ala-Ala + Phe 4-methylcoumarin 7-amide - ? 15822 3.4.21.92 Succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide + H2O ClpP subunit alone Escherichia coli RGC125 (lon-) Succinyl-Ala-Ala + Phe 4-methylcoumarin 7-amide - ? 15822 3.4.21.92 succinyl-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O recombinant mature ClpP is most active against succinyl-L-Leu-L-Lys-7-amido-4-methylcoumarin Plasmodium falciparum ? - ? 412925 3.4.21.92 succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O recombinant ClpP does not cleave the known ClpP substrate succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin Plasmodium falciparum succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin - ? 412928 3.4.21.92 Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O ClpP subunit alone Escherichia coli Succinyl-Leu + Leu + Val-Tyr 4-methylcoumarin 7-amide - ? 15823 3.4.21.92 Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O ClpP subunit alone Escherichia coli RGC125 (lon-) Succinyl-Leu + Leu + Val-Tyr 4-methylcoumarin 7-amide - ? 15823 3.4.21.92 Succinyl-Leu-Tyr 4-methylcoumarin 7-amide + H2O ClpP subunit alone Escherichia coli Succinyl-Leu-Tyr + 7-amino-4-methylcoumarin - ? 15821 3.4.21.92 succinyl-LLVY-7-amido-4-methylcoumarin + H2O - Plasmodium falciparum succinyl-LLVY + 7-amino-4-methylcoumarin - ? 362706 3.4.21.92 succinyl-LY-4-methylcoumarin-7-amide + H2O - Escherichia coli ? - ? 419101