| Type | Description |
|---|---|
| Definition | ATPase component of the HslVU protease |
| Date | Results | Publications |
|---|---|---|
| 2017-06-03 11:38:00 | a model in which ATP hydrolysis and linked mechanical function in the HslU ring operate by a probabilistic mechanism. | 28223361 |
| 2016-10-22 10:42:00 | The authors conclude that RcsA is indeed proteolized by ClpYQ protease. | 26856452 |
| 2012-12-22 11:12:00 | Transfer-messenger RNA-SmpB protein regulates ribonuclease R turnover by promoting binding of HslUV and Lon proteases | 22879590 |
| 2012-06-02 11:07:00 | The I domain plays an active role in coordinating substrate binding, ATP hydrolysis, and protein degradation by the HslUV proteolytic machine. | 22102327 |
| 2011-11-19 10:28:00 | Data revealed that an ATP-binding site in domain N, separate from its role in polypeptide (ClpY) oligomerization, is required for complex formation with ClpQ. | 21803990 |
| Type | IDs |
|---|---|
| Synonymous | ECK3923, clpY, htpI |
| Gene |
UniProtKB-ID:
HSLU_ECOLI
UniprotKB:
P0A6H5
UniParc:
UPI0000112FF5
EMBL:
AP009048,
U00096,
L19201
EnsemblGenome:
b3931,
BAE77379
KO:
eco:b3931,
ecj:JW3902
|
| Nucleutide sequences |
EMBL-CDS:
BAE77379.1,
AAC76913.1,
AAB03063.1
EnsemblGenome_TRS:
AAC76913,
BAE77379
|
| Protein sequencees |
EnsemblGenome_PRO:
BAE77379,
AAC76913
RefSeq:
NP_418366.1
|
| Others |
UniRef100:
UniRef100_P0A6H6
UniRef90:
UniRef90_P0A6H6
UniRef50:
UniRef50_P0A6H6
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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