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Information on EC 3.4.21.92 - Endopeptidase Clp and Organism(s) Synechococcus elongatus and UniProt Accession P54415

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.92 Endopeptidase Clp
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This record set is specific for:
Synechococcus elongatus
UNIPROT: P54415 not found.
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Word Map
The taxonomic range for the selected organisms is: Synechococcus elongatus
The enzyme appears in selected 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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP-dependent Clp protease
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-
-
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Caseinolytic protease
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-
-
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Clp protease
ClpCP3/R protease
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ClpP3
ClpP3/R complex
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endopeptidase Clp
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-
-
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endopeptidase Ti
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-
-
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Heat shock protein F21.5
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-
-
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Protease Ti
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-
-
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stress protein G7
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-casein + H2O
?
show the reaction diagram
-
is completely degraded by ClpC and ClpP3/R within 20 min
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-
?
chlorophyll + H2O
?
show the reaction diagram
-
-
-
-
?
FITC-casein + H2O
?
show the reaction diagram
-
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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-
?
FR-GFP + H2O
?
show the reaction diagram
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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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-
?
N-succinyl-Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O
N-succinyl-Ile-Ile-Trp + 7-amino-4-methylcoumarin
show the reaction diagram
-
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-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
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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-Val-Lys-Met-7-amido-4-methylcoumarin + H2O
N-succinyl-Val-Lys-Met + 7-amino-4-methylcoumarin
show the reaction diagram
-
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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-
?
additional information
?
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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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-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ClpP3/R complex stimulates the steady-state ATPase activity of ClpC
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
highly specific association between HSP100 chaperone ClpC and the ClpP3/R core. Two conserved sequences in the N-terminus of ClpR and one in the N-terminus of ClpP3 are crucial for the ClpC-ClpP3/R sdubunit association. These N-terminal domains also influence the stability of the ClpP3/R core complex itself. A unique C-terminal sequence just downstream of the P-loop region previously in ClpC confers specificity for the ClpP3/R core and prevents association with Escherichia coli ClpP
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
270000
300000
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gel filtration, ClpP1 and ClpP2
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heptamer
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single mixed heptameric ring of ClpP1 and ClpP2
oligomer
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ClpP3/R complex, SDS-PAGE
additional information
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Two soluble Clp proteolytic cores consisting of distinct pairs of ClpP/R paralogs, ClpP1/P2 and ClpP3/R exist in cyanobacteria. Each proteolytic core associates with a different HSP100 partner, ClpX with ClpP1/P2 and ClpC with ClpP3/R, ClpC with two ClpS adaptors.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of chaperone ClpC and ClpP3/R subunit structures. The R-ring of ClpP3 is most likely to associate with ClpC
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S101A
-
mutation of the active site Ser-101 in ClpP3 inactivates the entire ClpCP3/R protease, the mutation has no effect on the formation of the recombinant ClpP3/R core complex of 270 kDa. The mutated ClpP3/R complex stimulates the steady-state ATPase activity of ClpC to the same extent as wild-type ClpP3/R. The mutated ClpP3/R core fails to degrade the alpha-casein nor the more sensitive FITC-casein
additional information
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isoform ClpP1 inactivation mutant, little or no net degradation of chlorophyll under conditions that drive chlorophyll degradation in wild-type. Isoform ClpP2 inactivation mutant, chlorophyll degradation is similar to wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by immunoprecipitation
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ClpP3/R complex purified on Ni2+ affinity column and by gel filtration, purification of ClpC and ClpS1
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
clpP3 and clpR genes cloned into the pACYC Duet vector for co-expression in Escherichia coli BL21-STAR cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barker-Astrom, K.; Schelin, J.; Gustafsson, P.; Clarke, A.K.; Campbell, D.A.
Chlorosis during nitrogen starvation is altered by carbon dioxide and temperature status and is mediated by the ClpP1 protease in Synechococcus elongatus
Arch. Microbiol.
183
66-69
2005
Synechococcus elongatus
Manually annotated by BRENDA team
Stanne, T.M.; Pojidaeva, E.; Andersson, F.I.; Clarke, A.K.
Distinctive types of ATP-dependent Clp proteases in cyanobacteria
J. Biol. Chem.
282
14394-14402
2007
Synechococcus elongatus
Manually annotated by BRENDA team
Andersson, F.I.; Tryggvesson, A.; Sharon, M.; Diemand, A.V.; Classen, M.; Best, C.; Schmidt, R.; Schelin, J.; Stanne, T.M.; Bukau, B.; Robinson, C.V.; Witt, S.; Mogk, A.; Clarke, A.K.
Structure and function of a novel type of ATP-dependent CLP protease
J. Biol. Chem.
284
13519-13532
2009
Synechococcus elongatus
Manually annotated by BRENDA team
Tryggvesson, A.; Stahlberg, F.M.; Mogk, A.; Zeth, K.; Clarke, A.K.
Interaction specificity between the chaperone and proteolytic components of the cyanobacterial Clp protease
Biochem. J.
446
311-320
2012
Synechococcus elongatus (Q9L4P3), Synechococcus elongatus, Synechococcus elongatus PCC 7942 (Q9L4P3)
Manually annotated by BRENDA team