Difference between revisions of "RsbT"
| Line 63: | Line 63: | ||
=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
| − | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' phosphorylation of [[RsbR]], [[RsbRB]], [[RsbRC]], and [[RsbRD]] {{PubMed|21362065}} |
* '''Protein family:''' | * '''Protein family:''' | ||
| Line 81: | Line 81: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' [[RsbS]]-[[RsbT]] {{PubMed|16321960}}, [[RsbR]]-[[RsbT]], [[RsbT]]-[[RsbU]] | + | * '''Interactions:''' |
| + | ** [[RsbS]]-[[RsbT]] {{PubMed|16321960}}, [[RsbR]]-[[RsbT]] {{PubMed|21362065}}, [[RsbRB]]-[[RsbT]] {{PubMed|21362065}}, [[RsbRC]]-[[RsbT]] {{PubMed|21362065}}, [[RsbRD]]-[[RsbT]] {{PubMed|21362065}}, [[RsbT]]-[[RsbU]] | ||
| + | ** component of the [[stressosome]] | ||
* '''Localization:''' | * '''Localization:''' | ||
| Line 137: | Line 139: | ||
==Original Articles== | ==Original Articles== | ||
| + | '''Additional publications:''' {{PubMed|21362065}} | ||
<pubmed>8682789,8002610,8682769,9658013,17303566, 9786195,15090521,10781545, 15583165, 8824586, 10329124,16321960,8808936,15312768,11244072,15342582,20019076, 12499568, 12950928, 16321960, 8955331, 18832644</pubmed> | <pubmed>8682789,8002610,8682769,9658013,17303566, 9786195,15090521,10781545, 15583165, 8824586, 10329124,16321960,8808936,15312768,11244072,15342582,20019076, 12499568, 12950928, 16321960, 8955331, 18832644</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 15:50, 4 March 2011
- Description: PP2C activator, protein serine kinase, phosphorylates RsbS, part of the stressosome
| Gene name | rsbT |
| Synonyms | ycxT |
| Essential | no |
| Product | PP2C activator, protein serine kinase |
| Function | control of SigB activity |
| Metabolic function and regulation of this protein in SubtiPathways: Stress | |
| MW, pI | 14 kDa, 6.587 |
| Gene length, protein length | 399 bp, 133 aa |
| Immediate neighbours | rsbS, rsbU |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
protein modification, sigma factors and their control
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU04690
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 3VY9 (complete stressosome)
- UniProt: P42411
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation: constitutively expressed PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Bill Haldenwang, San Antonio, USA
- Chet Price, Davis, USA homepage
- Rick Lewis, Newcastle, UK homepage
Your additional remarks
References
Reviews
Jon Marles-Wright, Richard J Lewis
The stressosome: molecular architecture of a signalling hub.
Biochem Soc Trans: 2010, 38(4);928-33
[PubMed:20658979]
[WorldCat.org]
[DOI]
(I p)
Jon Marles-Wright, Richard J Lewis
The Bacillus subtilis stressosome: A signal integration and transduction hub.
Commun Integr Biol: 2008, 1(2);182-4
[PubMed:19704888]
[WorldCat.org]
[DOI]
(I p)
Jan Pané-Farré, Richard J Lewis, Jörg Stülke
The RsbRST stress module in bacteria: a signalling system that may interact with different output modules.
J Mol Microbiol Biotechnol: 2005, 9(2);65-76
[PubMed:16319496]
[WorldCat.org]
[DOI]
(P p)
Original Articles
Additional publications: PubMed
