Difference between revisions of "RsbR"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
{{SubtiWiki category|[[sigma factors and their control]]}}, | {{SubtiWiki category|[[sigma factors and their control]]}}, | ||
− | {{SubtiWiki category|[[phosphoproteins]]}} | + | {{SubtiWiki category|[[phosphoproteins]]}}, |
+ | [[most abundant proteins]] | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
− | * '''Domains:''' | + | * '''[[Domains]]:''' |
** RsbRA is composed of an N-terminal nonheme globin domain and a highly conserved C-terminal STAS (Sulphate Transporter and AntiSigma factor antagonist) domain. The C-terminal STAS domain is the target of the serine/threonine-specific kinase [[RsbT]] (see below). | ** RsbRA is composed of an N-terminal nonheme globin domain and a highly conserved C-terminal STAS (Sulphate Transporter and AntiSigma factor antagonist) domain. The C-terminal STAS domain is the target of the serine/threonine-specific kinase [[RsbT]] (see below). | ||
* '''Modification:''' phosphorylation on Thr-171 and Thr-205 by [[RsbT]] {{PubMed|21362065}} | * '''Modification:''' phosphorylation on Thr-171 and Thr-205 by [[RsbT]] {{PubMed|21362065}} | ||
− | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
Line 125: | Line 126: | ||
* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
Line 153: | Line 155: | ||
==Original Articles== | ==Original Articles== | ||
− | + | <pubmed>8002610,8682769,8682789, 17726680,10781545,15583165, 8824586,10329124,17158665, 9179850,8808936,15312768, 11244072,15342582,15378759, 12950928, 15466036, 9179850, 8955331, 18832644 ,17726680 ,17218307 20019076 21602359 23320651,21362065,20935101,22287516,22609918 </pubmed> | |
− | <pubmed>8002610,8682769,8682789, 17726680,10781545,15583165, 8824586,10329124,17158665, 9179850,8808936,15312768, 11244072,15342582,, 12950928, 15466036, 9179850, 8955331, 18832644 ,17726680 ,17218307 20019076 21602359 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 14:45, 5 March 2014
- Description: activator of RsbT kinase activity, stressosome sensor protein
Gene name | rsbR |
Synonyms | ycxR, rsbRA |
Essential | no |
Product | activator of RsbT kinase activity, stressosome sensor protein |
Function | control of SigB activity |
Gene expression levels in SubtiExpress: rsbR | |
Interactions involving this protein in SubtInteract: RbsR | |
Metabolic function and regulation of this protein in SubtiPathways: rsbR | |
MW, pI | 30 kDa, 4.731 |
Gene length, protein length | 822 bp, 274 aa |
Immediate neighbours | ndoA, rsbS |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
sigma factors and their control, phosphoproteins, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU04670
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
Extended information on the protein
- Kinetic information:
- Domains:
- RsbRA is composed of an N-terminal nonheme globin domain and a highly conserved C-terminal STAS (Sulphate Transporter and AntiSigma factor antagonist) domain. The C-terminal STAS domain is the target of the serine/threonine-specific kinase RsbT (see below).
- Effectors of protein activity:
- component of the stressosome
Database entries
- UniProt: P42409
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation: constitutively expressed PubMed
- Regulatory mechanism:
- Additional information:
- belongs to the 100 most abundant proteins PubMed
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
Marcel Jurk, Philipp Schramm, Peter Schmieder
The blue-light receptor YtvA from Bacillus subtilis is permanently incorporated into the stressosome independent of the illumination state.
Biochem Biophys Res Commun: 2013, 432(3);499-503
[PubMed:23416074]
[WorldCat.org]
[DOI]
(I p)
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