Difference between revisions of "RsbV"
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* '''Domains:''' | * '''Domains:''' | ||
| − | * '''Modification:''' phosphorylation on Ser-52 AND Ser-56 | + | * '''Modification:''' phosphorylation on Ser-52 AND Ser-56 by [[RsbW]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] |
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
| Line 70: | Line 70: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' [[RsbU]]-[[RsbV]], [[RsbV]]-[[SpoIIAB]], [[RsbV]]- | + | * '''Interactions:''' [[RsbU]]-[[RsbV]], [[RsbV]]-[[SpoIIAB]], [[RsbV]]-[[RsbW]][http://www.ncbi.nlm.nih.gov/sites/entrez/8144446 PubMed] |
* '''Localization:''' | * '''Localization:''' | ||
Revision as of 18:47, 31 May 2009
- Description: anti-anti-SigB, antagonist of RsbW
| Gene name | rsbV |
| Synonyms | |
| Essential | no |
| Product | anti-anti-SigB |
| Function | control of SigB activity |
| MW, pI | 11 kDa, 4.698 |
| Gene length, protein length | 327 bp, 109 aa |
| Immediate neighbours | rsbU, rsbW |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Coordinates:
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: STAS domain (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure: 1VC1 (homolog from Thermotoga maritima)
- Swiss prot entry: P17903
- KEGG entry: BSU04710
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680]
[WorldCat.org]
[DOI]
(P p)
Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307]
[WorldCat.org]
[DOI]
(P p)
A Petersohn, M Brigulla, S Haas, J D Hoheisel, U Völker, M Hecker
Global analysis of the general stress response of Bacillus subtilis.
J Bacteriol: 2001, 183(19);5617-31
[PubMed:11544224]
[WorldCat.org]
[DOI]
(P p)
U Voelker, A Voelker, W G Haldenwang
The yeast two-hybrid system detects interactions between Bacillus subtilis sigmaB regulators.
J Bacteriol: 1996, 178(23);7020-3
[PubMed:8955331]
[WorldCat.org]
[DOI]
(P p)
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
