RsbRD
- 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 |
Gene expression levels in SubtiExpress: rsbRD | |
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
| |
Expression at a glance PubMed 500px |
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:
- 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)
S Akbar, T A Gaidenko, C M Kang, M O'Reilly, K M Devine, C W Price
New family of regulators in the environmental signaling pathway which activates the general stress transcription factor sigma(B) of Bacillus subtilis.
J Bacteriol: 2001, 183(4);1329-38
[PubMed:11157946]
[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)