Bmr

• Description: general stress protein, multidrug-efflux transporter
  
  

Gene name	bmr
Synonyms	bmr1
Essential	no
Product	multidrug-efflux transporter
Function	multidrug resistance
Gene expression levels in SubtiExpress: bmr
MW, pI	42 kDa, 9.696
Gene length, protein length	1167 bp, 389 aa
Immediate neighbours	yqiW, bmrR
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• Expression browser: bmr 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)