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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
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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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-
?
Abz-KASPVSLGY(NO2)D + H2O
?
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-
-
-
?
alkaline phosphatase + H2O
?
-
-
-
-
?
alpha-casein + H2O
?
-
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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-
?
Arc-ssrA + H2O
peptides
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Arc repressor with a C-terminal ssrA tag
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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
-
-
-
-
?
casein + H2O
small peptides derived from casein
casein-fluorescein isothiocyanate + H2O
?
-
-
-
?
central competence regulator sigmax + H2O
?
chlorophyll + H2O
?
-
-
-
-
?
chlorophyllide a oxygenase + H2O
?
-
ClpC1 regulates the level of chlorophyllide a oxygenase, chloroplast ClpC1 regulates chlorophyll b biosynthesis
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-
?
CM-titin-ssrA + H2O
?
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-
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-
?
COMK + H2O
?
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ClpCP, MecA required
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-
?
copper transporter PAA2/HMA8 + H2O
?
elongation factor Ts + H2O
?
-
clpP6 mutant have impaired photosynthesis and chloroplast development
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-
?
fEGFP-ssrA + H2O
?
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
?
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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-
?
FlhC subunit + H2O + ATP
?
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
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-
?
GFP-K17 fusion protein + H2O
?
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-
-
-
?
GFP-ssrA + H2O
?
-
-
-
-
?
Glucagon + H2O
Hydrolyzed glucagon
Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-L-Arg + 7-amino-4-methylcoumarin
substrate for the recombinant ClpP
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?
green-fluorescent-protein-ssrA + H2O
?
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-
-
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?
insulin chain B + H2O
?
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-
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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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-
?
lambda O CM-titiin + H2O
?
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-
-
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?
Lambda O CM-titin + H2O
?
-
-
-
-
?
Leu-Tyr-Leu-Tyr-Trp + H2O
Leu-Tyr-Leu + Tyr-Trp
-
cleavage occurs primarily at Leu3-Tyr4, but significant cleavage also at Tyr2-Leu3 and Leu4-Trp5 bond
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?
LexA N-terminal domain + H2O
?
-
-
-
-
?
luciferase-ssrA + H2O
?
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-
-
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?
MurAA + H2O
?
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MecA not required for degradation
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-
?
Mutated repressor of Mu prophage + H2O
Hydrolyzed mutated repressor of Mu prophage
-
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
-
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
-
-
?
N-succinyl-L-isoleucine-L-isoleucine-L-tryptophan-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
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-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
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-
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?
N-succinyl-Val-Lys-Met-7-amido-4-methylcoumarin + H2O
N-succinyl-Val-Lys-Met + 7-amino-4-methylcoumarin
-
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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?
protein RepA + H2O
?
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model substrate from bacteriophage P1
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?
RNA Helicase + H2O
?
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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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?
RsiW + H2O
?
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ClXCP, AA at C-terminal as degradation tag
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?
Sda + H2O
?
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ClpXP, VSS at C-terminal as degradation tag
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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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?
Suc-AAPF-4-methylcoumarin-7-amide + H2O
?
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?
Suc-AFK-4-methylcoumarin-7-amide + H2O
?
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?
Suc-IA-4-methylcoumarin-7-amide + H2O
?
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?
Suc-IIW-4-methylcoumarin-7-amide + H2O
?
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?
Suc-LY-4-methylcoumarin-7-amide + H2O
?
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-
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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
?
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
-
ClpP subunit alone
-
?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-LY-4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
additional information
?
-
Bacteriophage lambdaO-DNA replication protein + H2O
Hydrolyzed bacteriophage lambdaO-DNA replication protein
-
degraded by ClpXP
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?
Bacteriophage lambdaO-DNA replication protein + H2O
Hydrolyzed bacteriophage lambdaO-DNA replication protein
-
degraded by ClpXP
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?
beta-casein + H2O
?
-
-
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?
beta-casein + H2O
?
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-
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?
beta-casein + H2O
?
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?
casein + H2O
?
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-
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?
casein + H2O
small peptides derived from casein
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-
-
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?
casein + H2O
small peptides derived from casein
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alpha-casein
-
?
casein + H2O
small peptides derived from casein
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-
-
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?
central competence regulator sigmax + H2O
?
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
?
adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner
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-
?
copper transporter PAA2/HMA8 + H2O
?
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?
copper transporter PAA2/HMA8 + H2O
?
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?
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
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-
?
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
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-
?
Glucagon + H2O
Hydrolyzed glucagon
-
cleavage at multiple sites
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-
?
Glucagon + H2O
Hydrolyzed glucagon
-
cleavage at multiple sites
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-
?
LacZ + H2O
?
-
proteolytic subunit ClpP2 over-expression induces degradation of untagged LacZ
-
?
LacZ + H2O
?
-
proteolytic subunit ClpP2 over-expression induces degradation of untagged LacZ
-
?
N-succinyl-Leu-Tyr 4-methylcoumarin 7-amide + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
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
?
-
initial degradation rate is the same within error for wild-type ClpP, ClpAP, and ClpPDELTAN
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
?
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-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + 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-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
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
-
-
?
Spx + H2O
?
-
ClpCP, MecA or YpbH required for degradation
-
-
?
Spx + H2O
?
-
ClpXP, LAN at C-terminal as degradation tag, MecA not required
-
-
?
SsrA-tagged LacZ + H2O
?
both proteolytic subunits ClpP1 and ClpP2 degrade SsrA-tagged LacZ
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-
?
SsrA-tagged LacZ + H2O
?
both proteolytic subunits ClpP1 and ClpP2 degrade SsrA-tagged LacZ
-
-
?
Succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide + H2O
Succinyl-Ala-Ala + Phe 4-methylcoumarin 7-amide
-
ClpP subunit alone
-
?
Succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide + H2O
Succinyl-Ala-Ala + Phe 4-methylcoumarin 7-amide
-
ClpP subunit alone
-
?
Succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide + H2O
Succinyl-Ala-Ala + Phe 4-methylcoumarin 7-amide
-
ClpP subunit alone
-
?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
Succinyl-Leu + Leu + Val-Tyr 4-methylcoumarin 7-amide
-
ClpP subunit alone
-
?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
Succinyl-Leu + Leu + Val-Tyr 4-methylcoumarin 7-amide
-
ClpP subunit alone
-
?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
Succinyl-Leu + Leu + Val-Tyr 4-methylcoumarin 7-amide
-
ClpP subunit alone
-
?
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
-
?
additional information
?
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stress- and starvation-induced bulk protein turnover depends virtually exclusively on enzyme, which is also essential for intracellular protein quality control
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-
?
additional information
?
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-
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
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-
?
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
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-
?
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
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-
?
additional information
?
-
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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
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?
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
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?
additional information
?
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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
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-
?
additional information
?
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-
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-
?
additional information
?
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-
role for the Clp protease in activating Mu-mediated DNA rearrangements
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?
additional information
?
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ClpP subunit has peptidase activity against very short peptides, with fewer than five amino acid residues in the absence of ClpA and nucleotide
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?
additional information
?
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-
when activated by ClpA subunit, ClpP can degrade longer polypeptides and proteins
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?
additional information
?
-
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physiological activation of Mu-dependent DNA rearrangements requires Clp functions. Clp plays a role in monitoring the physiological status of the cell
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?
additional information
?
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-
ClpXP appears to be involved in plasmid maintenance and in phage Mu virulence
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-
?
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
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?
additional information
?
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-
selectivity of degradation by ClpP in vivo is determined by interaction of ClpP with different regulatory ATPase subunits
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-
?
additional information
?
-
-
ClpP is present in a wide range of prokaryotic and eukaryotic cells and is highly conserved in plant chloroplasts
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-
?
additional information
?
-
-
removing of irreversibly damaged polypeptides
-
?
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
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-
?
additional information
?
-
-
ClpP associates with ClpX or ClpA to form the AAA+ ClpXP or ClpAP proteases
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-
?
additional information
?
-
-
ClpP binds to AAA+ ATPase/unfoldase, ClpA or ClpX
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-
?
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
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?
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
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?
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
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-
?
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
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-
?
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
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-
?
additional information
?
-
-
when activated by ClpA subunit, ClpP can degrade longer polypeptides and proteins
-
-
?
additional information
?
-
-
ClpXP appears to be involved in plasmid maintenance and in phage Mu virulence
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-
?
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
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-
?
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
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?
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
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?
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
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-
?
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
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-
?
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
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-
?
additional information
?
-
recombinant mature ClpP is not capable of hydrolyzing Gly-L-Arg-7-amido-4-methylcoumarin, GlyL-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
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-
?
additional information
?
-
-
recombinant mature ClpP is not capable of hydrolyzing Gly-L-Arg-7-amido-4-methylcoumarin, GlyL-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
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-
?
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
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?
additional information
?
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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
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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
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additional information
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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
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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
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enzyme is required for the growth at elevated temperature and for virulence
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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
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nasal immunizations with ClpP and CbpA are efficient for induction of systemic and mucosal antibodies
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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
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Bonnet, M.; Stegmann, M.; Maglica, Z.; Stiegeler, E.; Weber-Ban, E.; Hennecke, H.; Mesa, S.
FixK2, a key regulator in Bradyrhizobium japonicum, is a substrate for the protease ClpAP in vitro
FEBS Lett.
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2013
Bradyrhizobium japonicum (Q89KG1), Bradyrhizobium japonicum
brenda
Li, D.; Zhang, C.; Lu, N.; Mu, L.; He, Y.; Xu, L.; Yang, J.; Fan, Y.; Kang, Y.; Yang, C.
Cloning and characterization of Clp protease proteolytic subunit 2 and its implication in clinical diagnosis of tuberculosis
Int. J. Clin. Exp. Pathol.
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2014
Mycobacterium tuberculosis (P9WPC3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPC3)
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Gersch, M.; Kolb, R.; Alte, F.; Groll, M.; Sieber, S.A.
Disruption of oligomerization and dehydroalanine formation as mechanisms for ClpP protease inhibition
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Staphylococcus aureus
brenda
Wahl, A.; Servais, F.; Drucbert, A.S.; Foulon, C.; Fontaine, L.; Hols, P.
Control of natural transformation in salivarius Streptococci through specific degradation of sigmaX by the MecA-ClpCP protease complex
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Streptococcus thermophilus (Q5M6G1), Streptococcus thermophilus, Streptococcus thermophilus ATCC BAA-250 (Q5M6G1)
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Sato, Y.; Takaya, A.; Mouslim, C.; Hughes, K.T.; Yamamoto, T.
FliT selectively enhances proteolysis of FlhC subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP
J. Biol. Chem.
289
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2014
Salmonella enterica (Q8ZRC0), Salmonella enterica ATCC 700720 (Q8ZRC0)
brenda
Brzozowska, I.; Zielenkiewicz, U.
The ClpXP protease is responsible for the degradation of the Epsilon antidote to the Zeta toxin of the streptococcal pSM19035 plasmid
J. Biol. Chem.
289
7514-7523
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Bacillus subtilis
brenda
Bhat, N.H.; Vass, R.H.; Stoddard, P.R.; Shin, D.K.; Chien, P.
Identification of ClpP substrates in Caulobacter crescentus reveals a role for regulated proteolysis in bacterial development
Mol. Microbiol.
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Caulobacter vibrioides
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Gersch, M.; Famulla, K.; Dahmen, M.; Goebl, C.; Malik, I.; Richter, K.; Korotkov, V.S.; Sass, P.; Ruebsamen-Schaeff, H.; Madl, T.; Broetz-Oesterhelt, H.; Sieber, S.A.
AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control
Nat. Commun.
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6320
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Staphylococcus aureus (Q2G036), Staphylococcus aureus NCTC 8325 (Q2G036)
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Derrien, B.; Majeran, W.; Effantin, G.; Ebenezer, J.; Friso, G.; van Wijk, K.J.; Steven, A.C.; Maurizi, M.R.; Vallon, O.
The purification of the Chlamydomonas reinhardtii chloroplast ClpP complex: additional subunits and structural features
Plant Mol. Biol.
80
189-202
2012
Chlamydomonas reinhardtii
brenda
Xie, F.; Zhang, Y.; Li, G.; Zhou, L.; Liu, S.; Wang, C.
The ClpP protease is required for the stress tolerance and biofilm formation in Actinobacillus pleuropneumoniae
PLoS ONE
8
e53600
2013
Actinobacillus pleuropneumoniae
brenda
Personne, Y.; Brown, A.; Schuessler, D.; Parish, T.
Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities
PLoS ONE
8
e60228
2013
Mycobacterium tuberculosis (P9WPC3), Mycobacterium tuberculosis (P9WPC5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPC3), Mycobacterium tuberculosis H37Rv (P9WPC5)
brenda
Lee, J.O.; Kim, J.Y.; Rhee, D.K.; Pyo, S.
Streptococcus pneumoniae ClpP protease induces apoptosis via caspase-independent pathway in human neuroblastoma cells: cytoplasmic relocalization of p53
Toxicon
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Streptococcus pneumoniae
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Alexopoulos, J.A.; Guarne, A.; Ortega, J.
ClpP: a structurally dynamic protease regulated by AAA+ proteins
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2012
Escherichia coli (P0A6G7), Bacillus subtilis (P80244)
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Amor, A.J.; Schmitz, K.R.; Sello, J.K.; Baker, T.A.; Sauer, R.T.
Highly dynamic interactions maintain kinetic stability of the ClpXP protease during the ATP-fueled mechanical cycle
ACS Chem. Biol.
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1552-1560
2016
Escherichia coli (P0A6G7)
brenda
Ni, T.; Ye, F.; Liu, X.; Zhang, J.; Liu, H.; Li, J.; Zhang, Y.; Sun, Y.; Wang, M.; Luo, C.; Jiang, H.; Lan, L.; Gan, J.; Zhang, A.; Zhou, H.; Yang, C.G.
Characterization of gain-of-function mutant provides new insights into ClpP structure
ACS Chem. Biol.
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1964-1972
2016
Staphylococcus aureus (P63786), Staphylococcus aureus, Staphylococcus aureus MW2 (P63786)
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Choules, M.P.; Wolf, N.M.; Lee, H.; Anderson, J.R.; Grzelak, E.M.; Wang, Y.; Ma, R.; Gao, W.; McAlpine, J.B.; Jin, Y.Y.; Cheng, J.; Lee, H.; Suh, J.W.; Duc, N.M.; Paik, S.; Choe, J.H.; Jo, E.K.; Chang, C.L.; Lee, J.S.; Jaki, B.U.; Pauli, G.F.; Franzblau, S.G.; Cho, S.
Rufomycin targets ClpC1 proteolysis in Mycobacterium tuberculosis and M. abscessus
Antimicrob. Agents Chemother.
63
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2019
Mycobacterium tuberculosis (P9WPC5 and P9WPC3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPC5 and P9WPC3)
brenda
Aguado, A.; Fernandez-Higuero, J.A.; Cabrera, Y.; Moro, F.; Muga, A.
ClpB dynamics is driven by its ATPase cycle and regulated by the DnaK system and substrate proteins
Biochem. J.
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561-570
2015
Escherichia coli, Escherichia coli BB4561
brenda
Zhang, Y.; Maurizi, M.R.
Mitochondrial ClpP activity is required for cisplatin resistance in human cells
Biochim. Biophys. Acta
1862
252-264
2016
Homo sapiens (Q16740)
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Marsee, J.D.; Ridings, A.; Yu, T.; Miller, J.M.
Mycobacterium tuberculosis ClpC1 N-terminal domain is dispensable for adaptor protein-dependent allosteric regulation
Int. J. Mol. Sci.
19
3651
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Mycobacterium tuberculosis (P9WPC9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPC9)
brenda
Weinhaeupl, K.; Brennich, M.; Kazmaier, U.; Lelievre, J.; Ballell, L.; Goldberg, A.; Schanda, P.; Fraga, H.
The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis
J. Biol. Chem.
293
8379-8393
2018
Mycobacterium tuberculosis
brenda
Trentini, D.B.; Suskiewicz, M.J.; Heuck, A.; Kurzbauer, R.; Deszcz, L.; Mechtler, K.; Clausen, T.
Arginine phosphorylation marks proteins for degradation by a Clp protease
Nature
539
48-53
2016
Bacillus subtilis (P80244), Bacillus subtilis, Bacillus subtilis 168 (P80244)
brenda
Tapken, W.; Kim, J.; Nishimura, K.; van Wijk, K.; Pilon, M.
The Clp protease system is required for copper ion-dependent turnover of the PAA2/HMA8 copper transporter in chloroplasts
New Phytol.
205
511-517
2015
Arabidopsis thaliana, Arabidopsis thaliana Col-0
brenda
Leodolter, J.; Warweg, J.; Weber-Ban, E.
The Mycobacterium tuberculosis ClpP1P2 protease interacts asymmetrically with its ATPase partners ClpX and ClpC1
PLoS ONE
10
e0125345
2015
Mycobacterium tuberculosis (P9WPC5 and P9WPC3), Mycobacterium tuberculosis
brenda
Shi, X.; Wu, T.; M Cole, C.; K Devaraj, N.; Joseph, S.
Optimization of ClpXP activity and protein synthesis in an E. coli extract-based cell-free expression system
Sci. Rep.
8
3488
2018
Escherichia coli (P0A6G7), Escherichia coli
brenda
Sivertsson, E.M.; Jackson, S.E.; Itzhaki, L.S.
The AAA+ protease ClpXP can easily degrade a 31 and a 52-knotted protein
Sci. Rep.
9
2421
2019
Escherichia coli
brenda