Type | Description |
---|---|
Definition | ClpB chaperone |
Date | Results | Publications |
---|---|---|
2020-07-18 10:03:00 | ClpB activation reduces ATPase cooperativity and induces a sequential mode of ATP hydrolysis in the AAA2 ring, the main ATPase motor. | 31216466 |
2020-02-29 10:58:00 | Suggest possible role of E. coli ClpB in the molecular signaling cascade of protein-induced satiety. | 31491982 |
2019-10-12 10:39:00 | The authors find that large aggregates or bulky, native-like substrates activate the DnaK-ClpB complex, whereas a smaller, permanently unfolded protein or extended, short peptides fail to stimulate it. | 29643454 |
2017-06-24 10:10:00 | The authors show here that both Escherichia coli ClpB and Saccharomyces cerevisiae Hsp104 cooperation with their cognate Hsp70 is crucial for efficient protein disaggregation and, in contrast to earlier claims, cannot be circumvented by activating M-domain mutations. | 27616763 |
2016-10-29 10:07:00 | This unit describes the procedure for following reactivation of an aggregated enzyme glucose-6-phosphate dehydrogenase mediated by ClpB from Escherichia coli in cooperation with another molecular chaperone, DnaK. | 26836408 |
Type | IDs |
---|---|
Synonymous | ECK2590, htpM |
Gene |
UniProtKB-ID:
CLPB_ECOLI
UniprotKB:
P63284
UniParc:
UPI0000D7A472,
UPI0000127B0F
EMBL:
M29364,
V00350,
X57620,
AP009048,
U00096,
U50134
EnsemblGenome:
BAA16476,
b2592
KO:
ecj:JW2573,
eco:b2592
|
Nucleutide sequences |
EMBL-CDS:
CAA40846.1,
AAA24422.1,
AAC75641.1,
BAA16476.1,
CAA23639.1,
AAA92959.1
EnsemblGenome_TRS:
BAA16476,
AAC75641
|
Protein sequencees |
EnsemblGenome_PRO:
BAA16476,
AAC75641
RefSeq:
NP_417083.1
|
Others |
UniRef100:
UniRef100_P63285
UniRef90:
UniRef90_P63284-2
UniRef50:
UniRef50_P63284-2
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
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