3.6.4.10: non-chaperonin molecular chaperone ATPase
This is an abbreviated version!
For detailed information about non-chaperonin molecular chaperone ATPase, go to the full flat file.
Word Map on EC 3.6.4.10
-
3.6.4.10
-
client
-
endothelial
-
necrosis
-
proteasome
-
glucose-regulated
-
chaperonins
-
misfolded
-
chop
-
cardiac
-
ischemia
-
actin
-
caspase-3
-
lymphocyte
-
dismutase
-
artery
-
neurodegenerative
-
refolding
-
sirnas
-
cytoprotective
-
tnf
-
myocardial
-
autoimmune
-
neuroprotective
-
metastasis
-
bcl-2
-
steroid
-
hypoxia
-
glucocorticoid
-
reperfusion
-
hyperthermia
-
mapks
-
heat-induced
-
epitope
-
immunogen
-
mycobacterial
-
anti-apoptotic
-
stressor
-
cardiomyocytes
-
infarct
-
insult
-
parkinson
-
stress-related
-
precondition
-
tunel
-
perk
-
ischemia-reperfusion
-
cardioprotective
-
prion
-
chlamydia
-
raf-1
-
medicine
-
analysis
-
drug development
- 3.6.4.10
-
client
- endothelial
- necrosis
- proteasome
-
glucose-regulated
- chaperonins
-
misfolded
-
chop
- cardiac
- ischemia
- actin
- caspase-3
- lymphocyte
- dismutase
- artery
- neurodegenerative
-
refolding
- sirnas
-
cytoprotective
- tnf
- myocardial
- autoimmune
-
neuroprotective
- metastasis
- bcl-2
- steroid
- hypoxia
- glucocorticoid
-
reperfusion
- hyperthermia
- mapks
-
heat-induced
- epitope
- immunogen
-
mycobacterial
-
anti-apoptotic
-
stressor
- cardiomyocytes
- infarct
-
insult
- parkinson
-
stress-related
-
precondition
-
tunel
-
perk
-
ischemia-reperfusion
-
cardioprotective
- prion
- chlamydia
- raf-1
- medicine
- analysis
- drug development
Reaction
Synonyms
70 kD heat shock protein, 90 kDa heat shock protein, 90-kDa heat shock protein, AAA+ ATPase, AAA+ ATPase ClpB, AAA+ chaperone, AAA+ chaperone ClpB, ATP-dependent foldase, ATPase, ATPase chaperone, ATPase ClpB, bATPase, BiP, bona fide chaperone, chaperone ClpB, chaperone hsp90, chaperone Hsp90alpha, chaperone Hsp90beta, ClpB, ClpB ATPase, ClpB chaperone, ClpB disaggregase, ClpB1, ClpB2, ClpB2/HSP101, ClpC, ClpC chaperone, ClpX, ClpX heat-shock protein, disaggregase, DnaK, DnaK ATPase, DnaK chaperone, endoplasmic reticulum chaperone, ER lumenal hsc70 BiP, eukaryotic Hsc70 ATPase, GroEl, GRP75, Grp78, hATPase, heat shock cognate 70, heat shock cognate protein, heat shock protein, heat shock protein 70, heat shock protein 90, heat shock protein 90-alpha, heat shock protein GroEl, heat shock protein-70, heat shock protein-90, heat-shock cognate protein 70, heat-shock protein 70, heat-shock protein 90, Hsc66, Hsc70, Hsc82, Hsp100, HSP101, Hsp104, Hsp14.0, Hsp19.7, Hsp40, Hsp60, Hsp70, Hsp70 chaperone, Hsp70 chaperone Ssa1, Hsp70-1, Hsp70-2, Hsp70-3, HSP70.1, HSP70.2, Hsp82, Hsp82p, Hsp90, Hsp90 molecular chaperone, Hsp90a, Hsp90alpha, HSPA1L, HspA8, HspA9, HtpG, human alphabeta crystallin, human Hsp70 molecular chaperone, human stress70c, inducible heat shock protein 70, Kar2, maize stress70er, MecB protein, mitochondrial chaperone, mitochondrial heat shock protein 40, mitochondrial heat shock protein 70, mitochondrial heat-shock protein 70, mitochondrial hsp70, molecular chaperone, molecular chaperone BiP, molecular chaperone GroEl, molecular chaperone Hsc70 ATPase, mortalin, mortalin/mtHsp70, mouse alphabeta crystallin, mtHsp40, mtHSP70, p97-valosin-containing protein, p97-VCP, PBP74, PfClpB1, PfHsp70, PoHsp70, Pt-Hsp70, Ssq1, stress70 protein, SyClpC, tomato stress70c, vacuolar H+-ATPase, vacuolar membrane ATPase, yHsp90
ECTree
3.6.4.10 non-chaperonin molecular chaperone ATPaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.6.4.10 - non-chaperonin molecular chaperone ATPase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
V431F
-
mutant is unable to suppress the thermosensitivity of an Escherichia coli dnak103 deletion strain. Mutant is able to prevent the thermal aggregation of malate dehydrogenase
D526A
-
the DnaK mutant is unable to render a stimulated bichaperone complex with ClpB and doe s not reactivate glucose-6-phosphate dehydrogenase aggregates
E12C/E34A
-
mutant hydrolyses ATP about 10-times more slowly than wild-type protein, C for fluorescent labelling
E279A/K476C/E678A
site-directed mutagenesis, the mutant shows a reduced number of subunits
E34A
-
mutant hydrolyses ATP about 10-times more slowly than wild-type protein
F105W/W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
F276W/W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
F603W/W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
K476C
site-directed mutagenesis, the mutation weakens the dynamic interaction between M-domain and AAA1 ring resulting in M-domain dissociation and persistent, Hsp70-independent derepression of ClpB ATPase activity. Consequently, the ATPase activation by substrate is much stronger than in wild-type ClpB, and mutant ClpB-K476C has increased protein disaggregation activity, linked to its ability to unfold stable domains, an activity not observed for wild-type ClpB. ATP concentrations at half-maximal ATP hydrolysis rates of ClpB-K476C drop to 1.4 mM in the presence of substrate, compared with 4.3 mM for wild-type ClpB in the presence of substrate indicating that only the fully two-step activated state of ClpB reaches high ATPase activity at physiological ATP concentrations, which coincides with decreased cooperativity. Substrate-bound ClpB-K476C structures reveal large displacements of AAA2 pore loops
W462F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
Y251A/K476C
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to wild-type enzyme
Y251A/K476C/Y653A
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to wild-type enzyme
Y251W/W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
Y653A/K476C
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to wild-type enzyme
Y812/W462F/W543F
-
mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity
A116N
-
reduced affinity to co-chaperone Hop in the presence of ATP analogue AMPPNP
E371C
site-directed mutagenesis, the chaperone activity of ClpBE731C is similar to that of the wild-type protein
S433C
site-directed mutagenesis, the chaperone activity of ClpBS433C is similar to that of the wild-type protein
S499C
site-directed mutagenesis, the mutant shows 10-20fold increased ATPase activity, the chaperone activity of mutantt ClpBS499C is 20-25% more efficient than the wild-type
A107N
the mutation increases ATPase activity about 5fold compared to the wild type
C63A
-
the ATPase activity displayed by the unmodified ATPase domain Kar2 is fully maintained when Cys63 is replaced with Ala
C63F
-
the mutation leads to loss of ATPase activity. The mutation supports an enhanced viability during oxidative stress associated with the oxidized ATPase domain Kar2
C63H
-
the mutation supports an enhanced viability during oxidative stress associated with the oxidized ATPase domain Kar2
C63P
-
the mutation supports an enhanced viability during oxidative stress associated with the oxidized ATPase domain Kar2
C63V
-
the ATPase activity displayed by the unmodified ATPase domain Kar2 is fully maintained when Cys63 is replaced with Val
C63W
-
the mutation leads to loss of ATPase activity. The mutation leads to loss of ATPase activity. The mutation supports an enhanced viability during oxidative stress associated with the oxidized ATPase domain Kar2
C63Y
-
the mutation leads to loss of ATPase activity. The mutation supports an enhanced viability during oxidative stress associated with the oxidized ATPase domain Kar2
E285Q/E687Q
-
impaired hydrolysis of ATP at nucleotide-binding domains 1 and 2
E381K
-
no loss of ATPase activity at the non permissive temperature of 37°C
K199N
-
missense Sis1 mutant exhibits greatly reduced binding affinity for the Ssa1 lid domain
K202N
-
missense Sis1 mutant exhibits greatly reduced binding affinity for the Ssa1 lid domain
K214N
-
missense Sis1 mutant exhibits greatly reduced binding affinity for the Ssa1 lid domain
K218T
K620T
-
impaired binding and hydrolysis of ATP at nucleotide-binding domain 2
S25P
-
the mutation of Hsp82p impairs ATPase stimulation by Aha1p. The intrinsic ATPase activity of the mutant is comparable to that of wildtype enzyme
E271A/E668A
I403A/L406A/L413A/L420A/L432A/I439A/I446A/L449A
-
residues of hydrophobic interactions
I403A/L406A/L413A/L420A/L432A/I439A/I446A/L449A/I459A/L463A/L470A/V473A/I477A/L492A/L497A/L500A/L507A/L511A
-
residues of hydrophobic interactions
I459A/L463A/L470A/V473A/I477A/L492A/L497A/L500A/L507A/L511A
-
residues of hydrophobic interactions
L406A/L413A/L420A/L432A/I439A/I446A
-
residues of hydrophobic interactions
L406A/L413A/L420A/L432A/I439A/I446A/L463A/L470A/I477A/L492A/L500A/L507A
-
residues of hydrophobic interactions
L413A/L420A/L432A/I439A/L470A/I477A/L492A/L500A
-
residues of hydrophobic interactions
L463A/L470A/I477A/L492A/L500A/L507A
-
residues of hydrophobic interactions
additional information
K218T
-
impaired binding and hydrolysis of ATP at nucleotide-binding domain 1
additional information
-
in slothu45 mutant, the initial steps in sarcomere assembly take place, but thick filaments are absent and filamentous I-Z-I brushes fail to align or adopt correct spacing. The mutation only affects skeletal muscle and mutant embryos show no other obvious phenotypes. Phenotype is due to mutation in one copy of a tandemly duplicated hsp90a gene disrupting the chaperoning function through interference with aTPase activity. Loss of Hsp90a function leads to the downregulation of genes encoding sarcomeric proteins and upregulation of hsp90a and several other genes encoding proteins that may act with Hsp90a during sarcomere assembly
additional information
-
construction of DnaK /mtHsp70 chimeras by replacing different regions of the DnaK (from Escherichia coli) peptide-binding domain with those of mtHsp70 (from Saccharomyces cerevisiae) results in chimeric proteins that: (a) are not able to support growth of an Escherichia coli DnaK deletion strain at stress temperatures (e.g. 42°C), (b) show increased accessibility and decreased thermal stability of the peptide-binding pocket, and (c) have reduced activation by bacterial, but not mitochondrial cochaperones, as compared with DnaK
additional information
-
mutations in ATPase domain D2 significantly lowers enzyme activity
additional information
-
in vitro studies demonstrate that the N terminus of HSP70 including the ATPase domain and the substrate-binding beta-subdomain is not sufficient to bind with the J domain of HSJ1a. The C-terminal helical alpha-subdomain of HSP70 (residues 562610), is crucial for binding with the J domain of HSJ1a and stimulating the ATPase activity of HSP70
additional information
a mutant PoHsp70, PoHsp70M, that bears a mutation of the ATPase-associated domain, is completely abolished in activity. Construction of the DNA vaccine plasmids with wild-type and mutant enzymes, pSia10Hsp70 and pSia10Hsp70M. pSia10Hsp70 induces a survival rate that is significantly higher than that induced by pSia10, while pSia10Hsp70M induces a survival rate similar to that induced by pSia10
additional information
-
a mutant PoHsp70, PoHsp70M, that bears a mutation of the ATPase-associated domain, is completely abolished in activity. Construction of the DNA vaccine plasmids with wild-type and mutant enzymes, pSia10Hsp70 and pSia10Hsp70M. pSia10Hsp70 induces a survival rate that is significantly higher than that induced by pSia10, while pSia10Hsp70M induces a survival rate similar to that induced by pSia10
additional information
-
consstruction of a temperature-sensitive hsp70-2 knockout mutant
additional information
consstruction of a temperature-sensitive hsp70-2 knockout mutant
additional information
consstruction of a temperature-sensitive hsp70-2 knockout mutant
additional information
deletion of the N-terminal domain activates the basal activity 2fold, whereas elimination of the M domain increases the ATPase activity 10fold in the presence of casein. Attachment of fluorescent probes in the M domain and NBD2 does not affect the activity of ClpBS433C, it decreases that of ClpBE731C, especially when labelled with Alexa Fluor 350 (3fold reduction), and severely inhibits the ClpBS499C variant, overview
additional information
-
N-terminal deletion mutant DELTA8-Hsp90 still has ATPase activity that is not inhibited by Sti1
additional information
-
construction of DnaK /mtHsp70 chimeras by replacing different regions of the DnaK (from Escherichia coli) peptide-binding domain with those of mtHsp70 (from Saccharomyces cerevisiae) results in chimeric proteins that: (a) are not able to support growth of an Escherichia coli DnaK deletion strain at stress temperatures (e.g. 42°C), (b) show increased accessibility and decreased thermal stability of the peptide-binding pocket, and (c) have reduced activation by bacterial, but not mitochondrial cochaperones, as compared with DnaK
additional information
-
identification of 25 mutations within the two major cytosolic Hsp70-SSa molecular chaperones that impair the propagation of the [PSI+] prion. All but one mutation are located within the ATPase domain, and only mutation SSA2-A176T has major effects on growth rate
additional information
-
construction of a mutant mtHsp70A4, in which the linker residues of mtHsp70 are likewise replaced by four alanine residues. This variant generates in the folding assay only a 35-kD stable fragment that corresponds in size to the peptide-binding domain, the ATPase domain in the mtHsp70A4 mutant is not able to fold into a protease-resistant form
additional information
-
construction of C-terminal truncation and amino acid replacements in the IXI/V motif leading to loss of chaperone activity of all mutants at 83°C in contrast to the wild-type enzyme, both wild type and StHsp14.0WKW exhibit almost no significant change in secondary structure at high temperatures of 85°C and 50°C. Construction of an N-terminal truncation mutants of StHsp14.0, which form stable oligomeric complexes similar to that of the wild type, but exhibits reduced chaperone activity for the protection of thermophilic IPMDH from thermal aggregation
additional information
-
construction of C-terminal truncation and amino acid replacements in the IXI/V motif leading to loss of chaperone activity of all mutants at 83°C in contrast to the wild-type enzyme, both wild type and StHsp14.0WKW exhibit almost no significant change in secondary structure at high temperatures of 85°C and 50°C. Construction of an N-terminal truncation mutants of StHsp14.0, which form stable oligomeric complexes similar to that of the wild type, but exhibits reduced chaperone activity for the protection of thermophilic IPMDH from thermal aggregation
-
additional information
preparation of ordered heterohexamers of ClpB from Thermus thermophilus, in which two subunits having different mutations were cross-linked to each other and arranged alternately. ATPase activities of ordered heterohexamers with varyying mutations in the Walker A and B motifs, or the Arg-finger, of the two D domains, overview
additional information
-
preparation of ordered heterohexamers of ClpB from Thermus thermophilus, in which two subunits having different mutations were cross-linked to each other and arranged alternately. ATPase activities of ordered heterohexamers with varyying mutations in the Walker A and B motifs, or the Arg-finger, of the two D domains, overview
additional information
-
RNAi-mediated downregulation of mtHsp40, Cells depleted for mtHsp70/mtHsp40 machinery lose kDNA but does not disrupt the cell cycle, phenotype
additional information
-
RNAi-mediated downregulation of mtHsp70, cells depleted for mtHsp70/mtHsp40 machinery lose kDNA but does not disrupt the cell cycle, phenotype
