Bmr

• Description: general stress protein, multidrug-efflux transporter
  
  

Gene name	bmr
Synonyms	bmr1
Essential	no
Product	multidrug-efflux transporter
Function	multidrug resistance
MW, pI	42 kDa, 9.696
Gene length, protein length	1167 bp, 389 aa
Immediate neighbours	yqiW, bmrR
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

transporters/ other, general stress proteins (controlled by SigB), resistance against toxins/ antibiotics

This gene is a member of the following regulons

BmrR regulon, Mta regulon, SigB regulon

The gene

Basic information

• Locus tag: BSU24010

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: TCR/tet family (according to Swiss-Prot)

• Paralogous protein(s): Blt

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P33449

• 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:

References

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)