Difference between revisions of "Bmr"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU24010&redirect=T BSU24010]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/bmr.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/bmr.html]
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU24010&redirect=T BSU24010]
  
 
* '''Structure:'''
 
* '''Structure:'''

Revision as of 14:09, 2 April 2014

  • 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
Bmr context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Bmr expression.png
























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

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: 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:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • 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

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)