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
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3.4.21.92
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chloroplast
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adaptor
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tuberculosis
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mycobacterium
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atpases
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plastid
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aureus
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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
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caulobacter
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unfoldase
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proteostasis
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crescentus
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tetradecameric
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energy-dependent
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apicoplasts
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dnak
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self-compartmentalized
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n-degrons
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medicine
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ctra
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spx
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atp-fueled
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pyrazinamide
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toxin-antitoxin
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double-ring
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tmrna
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plastid-encoded
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barrel-shaped
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drug development
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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
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.21.92 - Endopeptidase Clp
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NATURAL SUBSTRATE 
NATURAL 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
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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?
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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-
?
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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?
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
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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
?
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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?
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
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?
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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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
?
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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
?
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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
?
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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
?
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removing of irreversibly damaged polypeptides
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?
additional information
?
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ClpP associates with ClpX or ClpA to form the AAA+ ClpXP or ClpAP proteases
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?
additional information
?
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ClpP binds to AAA+ ATPase/unfoldase, ClpA or ClpX
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?
additional information
?
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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
?
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ClpXP appears to be involved in plasmid maintenance and in phage Mu virulence
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?
additional information
?
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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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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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?
additional information
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enzyme is required for the growth at elevated temperature and for virulence
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?
