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Information on EC 3.6.4.10 - non-chaperonin molecular chaperone ATPase

for references in articles please use BRENDA:EC3.6.4.10
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EC Tree
IUBMB Comments
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.
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This record set is specific for:
UNIPROT: Q9RA63
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
hsp90, heat shock protein, grp78, hsp60, groel, molecular chaperone, heat shock protein 70, hsc70, heat shock protein 90, hsp40, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AAA+ chaperone ClpB
-
molecular chaperone Hsc70 ATPase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (polypeptide-polymerizing)
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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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
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
the enzyme collaborates with the DnaK chaperone system to dissolve protein aggregates both in vivo and in vitro
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-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
protein aggregate reactivation assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
intercalation of ATPase defective subunits into the hexamer every other subunit hampers its ATPase and disaggregation activities
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CLPB_THET8
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
854
0
96254
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterohexamer
a ring-shaped ClpB hexamer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E271Q/R576C/A821C
site-directed mutagenesis
E271Q/R576C/E668Q/A821C
site-directed mutagenesis
K204A/T205A/R576C/A821C
site-directed mutagenesis
K204A/T205A/R576C/K601A/K602A/A821C
site-directed mutagenesis
Q184C/A390C
site-directed mutagenesis
Q184C/A390C/E668Q
site-directed mutagenesis
Q184C/A390C/K601A/K602A
site-directed mutagenesis
Q184C/A390C/R747A
site-directed mutagenesis
Q184C/E271Q/A390C
site-directed mutagenesis
Q184C/E271Q/A390C/E668Q
site-directed mutagenesis
Q184C/K204A/T205A/A390C
site-directed mutagenesis
Q184C/K204A/T205A/A390C/K601A/K602A
site-directed mutagenesis
Q184C/R322A/A390C
site-directed mutagenesis
R322A/R576C/A821C
site-directed mutagenesis
R576C/A821C
site-directed mutagenesis
R576C/E668Q/A821C
site-directed mutagenesis
R576C/K601A/K602A/A821C
site-directed mutagenesis
R576C/R747A/A821C
site-directed mutagenesis
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography and Sephacryl S-200 gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamasaki, T.; Oohata, Y.; Nakamura, T.; Watanabe, Y.H.
Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement
J. Biol. Chem.
290
9789-9800
2015
Thermus thermophilus (Q9RA63), Thermus thermophilus
Manually annotated by BRENDA team
Rotanova, T.V.; Andrianova, A.G.; Kudzhaev, A.M.; Li, M.; Botos, I.; Wlodawer, A.; Gustchina, A.
New insights into structural and functional relationships between LonA proteases and ClpB chaperones
FEBS Open Bio
9
1536-1551
2019
Escherichia coli (P63284), Thermus thermophilus (Q9RA63)
Manually annotated by BRENDA team
Johnston, D.M.; Miot, M.; Hoskins, J.R.; Wickner, S.; Doyle, S.M.
Substrate discrimination by ClpB and Hsp104
Front. Mol. Biosci.
4
36
2017
Saccharomyces cerevisiae, Thermus thermophilus (Q9RA63)
Manually annotated by BRENDA team