BmrR

• Description: general stress protein, transcriptional activator of the bmr-bmrR operon
  
  

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

Categories containing this gene/protein

transcription factors and their control, general stress proteins (controlled by SigB), resistance against toxins/ antibiotics, membrane proteins

This gene is a member of the following regulons

BmrR regulon, Mta regulon, SigB regulon

The BmrR regulon:

• bmr-bmrR

The gene

Basic information

• Locus tag: BSU24020

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Structure: 2BOW (complex with effector), 1R8E (complex with DNA), 1BOW

• UniProt: P39075

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • bmrU-bmr-bmrR PubMed
  • bmr-bmrR PubMed

• Sigma factor:
  • bmrU: SigB PubMed
  • bmr: SigA PubMed

• Regulation:
  • bmrU: induced by stress (SigB) PubMed
  • bmr: induced by rhodamine 6G and tetraphenylphosphonium (BmrR) PubMed

• Regulatory mechanism:
  • BmrR: transcription activation PubMed
  • Mta: transcription activation PubMed

• 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

References

Sharrol Bachas, Christopher Eginton, Drew Gunio, Herschel Wade
Structural contributions to multidrug recognition in the multidrug resistance (MDR) gene regulator, BmrR.
Proc Natl Acad Sci U S A: 2011, 108(27);11046-51
[PubMed:21690368] [WorldCat.org] [DOI] (I p)

Muthiah Kumaraswami, Kate J Newberry, Richard G Brennan
Conformational plasticity of the coiled-coil domain of BmrR is required for bmr operator binding: the structure of unliganded BmrR.
J Mol Biol: 2010, 398(2);264-75
[PubMed:20230832] [WorldCat.org] [DOI] (I 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)

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)