3.4.21.92: Endopeptidase Clp
This is an abbreviated version!
For detailed information about Endopeptidase Clp, go to the full flat file.
Word Map on EC 3.4.21.92
-
3.4.21.92
-
chloroplast
-
adaptor
-
tuberculosis
-
mycobacterium
-
atpases
-
plastid
-
aureus
-
sigma
-
misfolded
-
hexamer
-
adeps
-
ssra-tagged
-
heptameric
-
caulobacter
-
unfoldase
-
proteostasis
-
crescentus
-
tetradecameric
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energy-dependent
-
apicoplasts
-
dnak
-
self-compartmentalized
-
n-degrons
-
medicine
-
ctra
-
spx
-
atp-fueled
-
pyrazinamide
-
toxin-antitoxin
-
double-ring
-
tmrna
-
plastid-encoded
-
barrel-shaped
-
drug development
-
analysis
- 3.4.21.92
- chloroplast
- adaptor
- tuberculosis
- mycobacterium
- atpases
- plastid
- aureus
- sigma
-
misfolded
-
hexamer
-
adeps
-
ssra-tagged
-
heptameric
- caulobacter
- unfoldase
-
proteostasis
- crescentus
-
tetradecameric
-
energy-dependent
- apicoplasts
- dnak
-
self-compartmentalized
-
n-degrons
- medicine
- ctra
- spx
-
atp-fueled
- pyrazinamide
-
toxin-antitoxin
-
double-ring
- tmrna
-
plastid-encoded
-
barrel-shaped
- drug development
- analysis
Reaction
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
ATP-dependent caseinolytic protease, ATP-dependent Clp protease, ATP-dependent Clp protease proteolytic subunit 1, ATP-dependent Clp protease proteolytic subunit 2, BsClpP, Caseinolytic protease, CLP, Clp protease, Clp proteolytic subunit, ClpA, ClpAP, ClpAP protease, ClpB, ClpC, ClpC ATPase, ClpC1, ClpCP protease, ClpCP3/R protease, ClpE, ClpP, ClpP Peptidase, ClpP Protease, ClpP protease complex, ClpP1, ClpP1 protease, ClpP1P2, ClpP2, ClpP2 protease, ClpP3, ClpP3/R complex, ClpQ, ClpR, ClpS1, ClpX, ClpX2, ClpXP, ClpXP protease, ClpY, CplC, endopeptidase Clp, endopeptidase Ti, Heat shock protein F21.5, heat-shock protease ClpP, nClpP7, nClpP8, PfClpP, Protease Ti, stress protein G7
ECTree
3.4.21.92 Endopeptidase ClpAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.21.92 - Endopeptidase Clp
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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
?
-
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
-
-
?
52-knotted ubiquitin C-terminal hydrolase L1-ssrA
?
-
substrate is fused to the 11-amino acid ssrA degron
-
-
?
alpha-casein + H2O
?
-
is completely degraded by ClpC and ClpP3/R within 20 min
-
-
?
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
-
-
?
Bacteriophage lambdaO-DNA replication protein + H2O
Hydrolyzed bacteriophage lambdaO-DNA replication protein
beta-Galactosidase fusion proteins + H2O
Hydrolyzed beta-galactosidase fusion protein
-
-
-
-
?
chlorophyllide a oxygenase + H2O
?
-
ClpC1 regulates the level of chlorophyllide a oxygenase, chloroplast ClpC1 regulates chlorophyll b biosynthesis
-
-
?
elongation factor Ts + H2O
?
-
clpP6 mutant have impaired photosynthesis and chloroplast development
-
-
?
fEGFP-ssrA + H2O
?
i.e. N-terminal His-tagged superfolder enhanced green fluorescent protein with the ssrA tag sequence at the C-terminus
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-L-Arg + 7-amino-4-methylcoumarin
substrate for the recombinant ClpP
-
-
?
Lambda O Arc + H2O
?
-
Arc repressor with a N-terminal lambda O degradation tag
-
-
?
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
-
?
Mutated repressor of Mu prophage + H2O
Hydrolyzed mutated repressor of Mu prophage
-
high susceptibility to the Clp-dependent degradation
-
-
?
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-amino-4-methylcoumarin
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
-
-
?
ornithine decarboxylase CC030 + H2O
?
-
-
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
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
cleavage at multiple sites
-
-
?
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
-
-
?
RpoS sigma factor + H2O
?
-
with the assistance of recognition factor RssB, ClpXP degrades the RpoS sigma factor
-
-
?
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
-
-
?
SsrA tagged proteins + H2O
?
-
ClpXP, AA at C-terminal as degradation tag
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
-
?
Bacteriophage lambdaO-DNA replication protein + H2O
Hydrolyzed bacteriophage lambdaO-DNA replication protein
-
degraded by ClpXP
-
-
?
Bacteriophage lambdaO-DNA replication protein + H2O
Hydrolyzed bacteriophage lambdaO-DNA replication protein
-
degraded by ClpXP
-
-
?
casein + H2O
small peptides derived from casein
-
-
-
-
?
central competence regulator sigmax + H2O
?
adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner
-
-
?
central competence regulator sigmax + H2O
?
adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner
-
-
?
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
-
-
?
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
-
-
?
Glucagon + H2O
Hydrolyzed glucagon
-
cleavage at multiple sites
-
-
?
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
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
?
-
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
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
ClpP linked to many activities, including sporulation, cell competence, stress tolerance and regulation of gene expression
-
?
additional information
?
-
-
stress- and starvation-induced bulk protein turnover depends virtually exclusively on enzyme, which is also essential for intracellular protein quality control
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
role for the Clp protease in activating Mu-mediated DNA rearrangements
-
-
?
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
-
-
?
additional information
?
-
-
when activated by ClpA subunit, ClpP can degrade longer polypeptides and proteins
-
-
?
additional information
?
-
-
physiological activation of Mu-dependent DNA rearrangements requires Clp functions. Clp plays a role in monitoring the physiological status of the cell
-
-
?
additional information
?
-
-
ClpXP appears to be involved in plasmid maintenance and in phage Mu virulence
-
-
?
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
-
-
?
additional information
?
-
-
selectivity of degradation by ClpP in vivo is determined by interaction of ClpP with different regulatory ATPase subunits
-
-
?
additional information
?
-
-
ClpP is present in a wide range of prokaryotic and eukaryotic cells and is highly conserved in plant chloroplasts
-
-
?
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
-
-
?
additional information
?
-
-
ClpP associates with ClpX or ClpA to form the AAA+ ClpXP or ClpAP proteases
-
-
?
additional information
?
-
-
ClpP binds to AAA+ ATPase/unfoldase, ClpA or ClpX
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
?
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-
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
-
-
?
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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-
?
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
?
-
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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-
?
additional information
?
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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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