Difference between revisions of "RsbQ"
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|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[SigB]] activity | |style="background:#ABCDEF;" align="center"|'''Function''' || control of [[SigB]] activity | ||
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU34100 rsbQ] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/RsbQ RsbQ] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/RsbQ RsbQ] | ||
| Line 26: | Line 26: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yvfR]]'', ''[[rsbP]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yvfR]]'', ''[[rsbP]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU34100 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU34100 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU34100 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:rsbQ_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:rsbQ_context.gif]] | ||
Revision as of 13:53, 13 May 2013
- Description: alpha/beta hydrolase, required for RsbP activation
| Gene name | rsbQ |
| Synonyms | yvfQ |
| Essential | no |
| Product | alpha/beta hydrolase |
| Function | control of SigB activity |
| Gene expression levels in SubtiExpress: rsbQ | |
| Interactions involving this protein in SubtInteract: RsbQ | |
| Metabolic function and regulation of this protein in SubtiPathways: Stress | |
| MW, pI | 29 kDa, 5 |
| Gene length, protein length | 807 bp, 269 aa |
| Immediate neighbours | yvfR, rsbP |
| Sequences | Protein DNA Advanced_DNA |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU34100
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: AB hydrolase superfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- UniProt: O07015
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Chet Price, Davis, USA homepage
Your additional remarks
References
Additional publications: PubMed
Locke JC, Young JW, Fontes M, Hernández Jiménez MJ, Elowitz MB Stochastic pulse regulation in bacterial stress response. Science. 2011 334:366-369. PubMed:21979936
Margaret S Brody, Valley Stewart, Chester W Price
Bypass suppression analysis maps the signalling pathway within a multidomain protein: the RsbP energy stress phosphatase 2C from Bacillus subtilis.
Mol Microbiol: 2009, 72(5);1221-34
[PubMed:19432806]
[WorldCat.org]
[DOI]
(I p)
Tomonori Kaneko, Nobuo Tanaka, Takashi Kumasaka
Crystal structures of RsbQ, a stress-response regulator in Bacillus subtilis.
Protein Sci: 2005, 14(2);558-65
[PubMed:15632289]
[WorldCat.org]
[DOI]
(P p)
M S Brody, K Vijay, C W Price
Catalytic function of an alpha/beta hydrolase is required for energy stress activation of the sigma(B) transcription factor in Bacillus subtilis.
J Bacteriol: 2001, 183(21);6422-8
[PubMed:11591687]
[WorldCat.org]
[DOI]
(P p)
