Difference between revisions of "RsbRD"
(→Extended information on the protein) |
|||
Line 49: | Line 49: | ||
* '''Locus tag:''' BSU24760 | * '''Locus tag:''' BSU24760 | ||
+ | |||
+ | [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rsbRD_2562966_2563802_-1 Expression] | ||
===Phenotypes of a mutant === | ===Phenotypes of a mutant === |
Revision as of 13:38, 25 January 2012
- Description: probably part of the stressosome, negative regulator of SigB activity
Gene name | rsbRD |
Synonyms | yqhA |
Essential | no |
Product | RsbR paralog |
Function | control of SigB activity |
Interactions involving this protein in SubtInteract: RsbRD | |
MW, pI | 31 kDa, 5.089 |
Gene length, protein length | 834 bp, 278 aa |
Immediate neighbours | yqhB, trnSL-Gln1 |
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
sigma factors and their control, general stress proteins (controlled by SigB), membrane proteins, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU24760
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:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- RsbRD-RsbT PubMed
- component of the stressosome
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P54504
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: rsbRD (according to DBTBS)
- 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
Additional publications: PubMed
Adam Reeves, Luis Martinez, William Haldenwang
Expression of, and in vivo stressosome formation by, single members of the RsbR protein family in Bacillus subtilis.
Microbiology (Reading): 2010, 156(Pt 4);990-998
[PubMed:20019076]
[WorldCat.org]
[DOI]
(I p)
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)
Tae-Jong Kim, Tatiana A Gaidenko, Chester W Price
A multicomponent protein complex mediates environmental stress signaling in Bacillus subtilis.
J Mol Biol: 2004, 341(1);135-50
[PubMed:15312768]
[WorldCat.org]
[DOI]
(P p)
A Petersohn, J Bernhardt, U Gerth, D Höper, T Koburger, U Völker, M Hecker
Identification of sigma(B)-dependent genes in Bacillus subtilis using a promoter consensus-directed search and oligonucleotide hybridization.
J Bacteriol: 1999, 181(18);5718-24
[PubMed:10482513]
[WorldCat.org]
[DOI]
(P p)