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Information on EC 3.4.21.92 - Endopeptidase Clp
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3.4.21.92 Endopeptidase ClpSpecify your search results
Word Map
- 3.4.21.92
- chloroplast
- adaptor
- tuberculosis
- mycobacterium
- atpases
- plastid
- aureus
- sigma
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misfolded
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hexamer
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adeps
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ssra-tagged
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heptameric
- caulobacter
- unfoldase
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proteostasis
- crescentus
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tetradecameric
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energy-dependent
- apicoplasts
- dnak
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self-compartmentalized
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n-degrons
- medicine
- ctra
- spx
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atp-fueled
- pyrazinamide
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toxin-antitoxin
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double-ring
- tmrna
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plastid-encoded
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barrel-shaped
- drug development
- analysis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-Tyr-/-NHMec, and Leu-Tyr-Leu-/-Tyr-Trp, in which cleavage of the -Tyr-/-Leu- and -Tyr-/-Trp bonds also occurs)
Synonyms
clp protease, clpap, clpxp protease, clpc1, clpp1, caseinolytic protease, clpp protease, clpp2, clpp1p2, atp-dependent clp protease, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP-dependent Clp protease
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ATP-dependent Clp protease proteolytic subunit 1
ATP-dependent Clp protease proteolytic subunit 2
Caseinolytic protease
CLP
Clp protease
Clp proteolytic subunit
ClpA
ClpAP
ClpC
ClpC1
ClpP
ClpP Peptidase
ClpP Protease
ClpP1
ClpP2
ClpP3
ClpS1
ClpX
ClpXP
CplC
endopeptidase Clp
endopeptidase Ti
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Heat shock protein F21.5
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Protease Ti
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stress protein G7
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Caseinolytic protease
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Clp protease
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ClpP
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ClpP
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cyanobacteria have many ClpP paralogs plus a ClpP variant, ClpP1, ClpP2, ClpP3, ClpR, ClpX, ClpS1 and ClpS2
endopeptidase Clp
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-Tyr-/-NHMec, and Leu-Tyr-Leu-/-Tyr-Trp, in which cleavage of the -Tyr-/-Leu- and -Tyr-/-Trp bonds also occurs)
Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-Tyr-/-NHMec; and Leu-Tyr-Leu-/-Tyr-Trp, in which cleavage of the -Tyr-/-Leu- and -Tyr-/-Trp bonds also occurs)
in presence of ATP and Mg2+. In the absence of ATP only oligopeptides shorter than five residues are hydrolyzed
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Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-Tyr-/-NHMec, and Leu-Tyr-Leu-/-Tyr-Trp, in which cleavage of the -Tyr-/-Leu- and -Tyr-/-Trp bonds also occurs)
dual mechanism in which translocation alternates with proteolysis, allowing peptides of more or less unifirm length to be cleaved processively from a translocating substrate
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Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-Tyr-/-NHMec, and Leu-Tyr-Leu-/-Tyr-Trp, in which cleavage of the -Tyr-/-Leu- and -Tyr-/-Trp bonds also occurs)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
110910-59-3
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131017-00-0
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131017-01-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
31-knotted methyltransferase YbeA-ssrA + H2O
?
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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
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?
52-knotted ubiquitin C-terminal hydrolase L1-ssrA
?
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substrate is fused to the 11-amino acid ssrA degron
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?
alpha-casein + H2O
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is completely degraded by ClpC and ClpP3/R within 20 min
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?
antitoxin epsilon + H2O
?
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Epsilon is an antitoxin of the Epsilon/Zeta toxin-antitoxin system family, purified Zeta toxin protects the Epsilon protein from rapid ClpXP-catalyzed degradation
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?
Bacteriophage lambdaO-DNA replication protein + H2O
Hydrolyzed bacteriophage lambdaO-DNA replication protein
beta-Galactosidase fusion proteins + H2O
Hydrolyzed beta-galactosidase fusion protein
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?
chlorophyllide a oxygenase + H2O
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ClpC1 regulates the level of chlorophyllide a oxygenase, chloroplast ClpC1 regulates chlorophyll b biosynthesis
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?
elongation factor Ts + H2O
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clpP6 mutant have impaired photosynthesis and chloroplast development
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?
fEGFP-ssrA + H2O
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i.e. N-terminal His-tagged superfolder enhanced green fluorescent protein with the ssrA tag sequence at the C-terminus
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?
FITC-casein + H2O
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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
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?
FixK2 + H2O
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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
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?
FR-GFP + H2O
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ClpCP3/R with ClpS1 take over 20 min to completely degrade FR-GFP, whereas the ClpAP protease degrades all FR-GFP within 2 min
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?
Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-L-Arg + 7-amino-4-methylcoumarin
substrate for the recombinant ClpP
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?
Lambda O Arc + H2O
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Arc repressor with a N-terminal lambda O degradation tag
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?
Leu-Tyr-Leu-Tyr-Trp + H2O
Leu-Tyr-Leu + Tyr-Trp
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cleavage occurs primarily at Leu3-Tyr4, but significant cleavage also at Tyr2-Leu3 and Leu4-Trp5 bond
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?
Mutated repressor of Mu prophage + H2O
Hydrolyzed mutated repressor of Mu prophage
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high susceptibility to the Clp-dependent degradation
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?
N-succinyl-Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O
N-succinyl-Ile-Ile-Trp + 7-amino-4-methylcoumarin
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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
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?
N-succinyl-L-isoleucine-L-isoleucine-L-tryptophan-7-amido-4-methylcoumarin + H2O
?
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?
N-succinyl-Leu-Tyr 4-methylcoumarin 7-amide + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
N-succinyl-Val-Lys-Met-7-amido-4-methylcoumarin + H2O
N-succinyl-Val-Lys-Met + 7-amino-4-methylcoumarin
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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
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?
ornithine decarboxylase CC030 + H2O
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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
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?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
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cleavage at multiple sites
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?
Phe-Ala-Pro-His-Met-Ala-Leu-Val-Pro-Val + H2O
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synthetic polypeptide that corresponds to the 10 amino acids surrounding the in vivo processing site in ClpP subunit
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?
RpoS sigma factor + H2O
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with the assistance of recognition factor RssB, ClpXP degrades the RpoS sigma factor
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SpollAB + H2O
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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
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?
SsrA tagged proteins + H2O
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ClpXP, AA at C-terminal as degradation tag
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?
ssrA-dabsyl + H2O
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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
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?
stalk synthesis transcription factor TacA + H2O
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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
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Starvation proteins + H2O
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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
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?
Succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide + H2O
Succinyl-Ala-Ala + Phe 4-methylcoumarin 7-amide
succinyl-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
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recombinant mature ClpP is most active against succinyl-L-Leu-L-Lys-7-amido-4-methylcoumarin
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?
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
recombinant ClpP does not cleave the known ClpP substrate succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin
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?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
Succinyl-Leu + Leu + Val-Tyr 4-methylcoumarin 7-amide
Succinyl-Leu-Tyr 4-methylcoumarin 7-amide + H2O
Succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
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ClpP subunit alone
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?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
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?
Bacteriophage lambdaO-DNA replication protein + H2O
Hydrolyzed bacteriophage lambdaO-DNA replication protein
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degraded by ClpXP
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?
Bacteriophage lambdaO-DNA replication protein + H2O
Hydrolyzed bacteriophage lambdaO-DNA replication protein
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degraded by ClpXP
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?
casein + H2O
small peptides derived from casein
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?
central competence regulator sigmax + H2O
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adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner
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?
central competence regulator sigmax + H2O
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adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner
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FlhC subunit + H2O + ATP
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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
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FlhC subunit + H2O + ATP
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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
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?
Glucagon + H2O
Hydrolyzed glucagon
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cleavage at multiple sites
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?
LacZ + H2O
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proteolytic subunit ClpP2 over-expression induces degradation of untagged LacZ
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?
LacZ + H2O
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proteolytic subunit ClpP2 over-expression induces degradation of untagged LacZ
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?
N-succinyl-Leu-Tyr 4-methylcoumarin 7-amide + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
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?
N-succinyl-Leu-Tyr 4-methylcoumarin 7-amide + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
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?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
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initial degradation rate is the same within error for wild-type ClpP, ClpAP, and ClpPDELTAN
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?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
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?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
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?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
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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
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?
Spx + H2O
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ClpXP, LAN at C-terminal as degradation tag, MecA not required
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?
SsrA-tagged LacZ + H2O
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both proteolytic subunits ClpP1 and ClpP2 degrade SsrA-tagged LacZ
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?
SsrA-tagged LacZ + H2O
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both proteolytic subunits ClpP1 and ClpP2 degrade SsrA-tagged LacZ
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?
Succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide + H2O
Succinyl-Ala-Ala + Phe 4-methylcoumarin 7-amide
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ClpP subunit alone
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?
Succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide + H2O
Succinyl-Ala-Ala + Phe 4-methylcoumarin 7-amide
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ClpP subunit alone
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?
Succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide + H2O
Succinyl-Ala-Ala + Phe 4-methylcoumarin 7-amide
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ClpP subunit alone
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?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
Succinyl-Leu + Leu + Val-Tyr 4-methylcoumarin 7-amide
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ClpP subunit alone
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?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
Succinyl-Leu + Leu + Val-Tyr 4-methylcoumarin 7-amide
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ClpP subunit alone
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?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
Succinyl-Leu + Leu + Val-Tyr 4-methylcoumarin 7-amide
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ClpP subunit alone
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?
additional information
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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
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additional information
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ClpP linked to many activities, including sporulation, cell competence, stress tolerance and regulation of gene expression