Difference between revisions of "BmrR"
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| − | * '''Description:''' general stress protein, transcriptional activator of the bmrU-bmrR operon <br/><br/> | + | * '''Description:''' general stress protein, transcriptional activator of the ''[[bmrU]]-[[bmr]]-[[bmrR]]'' operon <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
| Line 89: | Line 89: | ||
* '''Operon:''' | * '''Operon:''' | ||
| + | ** ''[[bmrU]]-[[bmr]]-[[bmrR]]'' {{PubMed|10220166}} | ||
| + | ** ''[[bmr]]-[[bmrR]]'' {{PubMed|7961792}} | ||
| − | * '''[[Sigma factor]]:''' [[SigB]] [http://www.ncbi.nlm.nih.gov/pubmed/11544224 PubMed] | + | * '''[[Sigma factor]]:''' |
| + | ** ''[[bmrU]]'': [[SigB]] [http://www.ncbi.nlm.nih.gov/pubmed/11544224 PubMed] | ||
| + | ** ''[[bmr]]'': [[SigA]] {{PubMed|10200972}} | ||
| − | * '''Regulation:''' induced by stress ([[SigB]]) [http://www.ncbi.nlm.nih.gov/pubmed/11544224 PubMed] | + | * '''Regulation:''' |
| + | ** ''[[bmrU]]'': induced by stress ([[SigB]]) [http://www.ncbi.nlm.nih.gov/pubmed/11544224 PubMed] | ||
| + | ** ''[[bmr]]'': induced by rhodamine 6G and tetraphenylphosphonium ([[BmrR]]) {{PubMed|7961792}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| + | ** [[BmrR]]: transcription activation {{PubMed|7961792}} | ||
| + | ** [[Mta]]: transcription activation {{PubMed|10200972}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
| Line 120: | Line 128: | ||
=References= | =References= | ||
| − | <pubmed>7608059,,11544224, </pubmed> | + | <pubmed>7608059,10220166,11544224, 7961792 10200972</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 21:14, 19 November 2009
| Gene name | bmrR |
| Synonyms | |
| Essential | no |
| Product | transcriptional activator |
| Function | regulation of multidrug resistance |
| MW, pI | 32 kDa, 5.187 |
| Gene length, protein length | 834 bp, 278 aa |
| Immediate neighbours | bmr, bkdB |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU24020
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:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- UniProt: P39075
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Richard Brennan, Houston, Texas, USA Homepage
Your additional remarks
References
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)
Anja Petersohn, Haike Antelmann, Ulf Gerth, Michael Hecker
Identification and transcriptional analysis of new members of the sigmaB regulon in Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 4);869-880
[PubMed:10220166]
[WorldCat.org]
[DOI]
(P p)
N N Baranova, A Danchin, A A Neyfakh
Mta, a global MerR-type regulator of the Bacillus subtilis multidrug-efflux transporters.
Mol Microbiol: 1999, 31(5);1549-59
[PubMed:10200972]
[WorldCat.org]
[DOI]
(P p)
M Ahmed, L Lyass, P N Markham, S S Taylor, N Vázquez-Laslop, A A Neyfakh
Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated.
J Bacteriol: 1995, 177(14);3904-10
[PubMed:7608059]
[WorldCat.org]
[DOI]
(P p)
M Ahmed, C M Borsch, S S Taylor, N Vázquez-Laslop, A A Neyfakh
A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates.
J Biol Chem: 1994, 269(45);28506-13
[PubMed:7961792]
[WorldCat.org]
(P p)
