Type | Description |
---|---|
Definition | cochaperonin GroES |
Date | Results | Publications |
---|---|---|
2019-01-05 10:16:00 | While GroEL and GroES increases the folding rate of PepQ by over 15-fold, the slow spontaneous folding of PepQ is not caused by aggregation. | 28665408 |
2014-04-19 11:07:00 | Evidence is provided for an interaction between GroESL and CspC that results in enhanced, temperature-dependent proteolysis of the latter. | 24148697 |
2013-02-09 11:38:00 | Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes | 23048033 |
2012-03-31 11:48:00 | Studies indicate that the amount of GroEL and GroES in an E. coli cell under normal conditions is sufficient to assist in the folding of no more than 5% of the proteins within the cell. | 22177460 |
2011-10-29 10:21:00 | substrate folding activity of a single ring GroEL variant is stimulated by modulating the cochaperonin GroES | 21757689 |
Type | IDs |
---|---|
Synonymous | ECK4136, groES, mopB |
Gene |
UniProtKB-ID:
CH10_ECOLI
UniprotKB:
P0A6F9
UniParc:
UPI0000000ED3
EMBL:
U14003,
X07850,
AP009048,
X07899,
U00096
EnsemblGenome:
BAE78144,
b4142
KO:
ecj:JW4102,
eco:b4142
|
Nucleutide sequences |
EMBL-CDS:
AAC77102.1,
BAE78144.1,
AAA97041.1,
CAA30697.1,
CAA30738.1
EnsemblGenome_TRS:
AAC77102,
BAE78144
|
Protein sequencees |
EnsemblGenome_PRO:
AAC77102,
BAE78144
RefSeq:
NP_418566.1
|
Others |
UniRef100:
UniRef100_A7ZV11
UniRef90:
UniRef90_A4W5N7
UniRef50:
UniRef50_O33499
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
---|---|---|---|---|---|---|---|---|
Refseq |
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