Difference between revisions of "BmrA"

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|style="background:#ABCDEF;" align="center"|'''Function''' || multiple antibiotic resistance
 
|style="background:#ABCDEF;" align="center"|'''Function''' || multiple antibiotic resistance
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU34820 bmrA]
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 64 kDa, 6.474   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 64 kDa, 6.474   

Revision as of 16:21, 7 August 2012

Gene name bmrA
Synonyms yvcC
Essential no
Product multidrug ABC transporter (ATP-binding protein)
Function multiple antibiotic resistance
Gene expression levels in SubtiExpress: bmrA
MW, pI 64 kDa, 6.474
Gene length, protein length 1767 bp, 589 aa
Immediate neighbours yvcD, yvzA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YvcC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
BmrA expression.png
























Categories containing this gene/protein

ABC transporters, resistance against toxins/ antibiotics, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU34820

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains: has both a membrane-spanning and an ATP-binding domain PubMed
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation: constitutively expressed PubMed
  • Regulatory mechanism:
  • Additional information:
    • half-life of the mRNA: 1.5 min PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Kerry J Lee, Lauren M Browning, Tao Huang, Feng Ding, Prakash D Nallathamby, Xiao-Hong Nancy Xu
Probing of multidrug ABC membrane transporters of single living cells using single plasmonic nanoparticle optical probes.
Anal Bioanal Chem: 2010, 397(8);3317-28
[PubMed:20544182] [WorldCat.org] [DOI] (I p)

Cédric Orelle, Francesca Gubellini, Anne Durand, Sergio Marco, Daniel Lévy, Philippe Gros, Attilio Di Pietro, Jean-Michel Jault
Conformational change induced by ATP binding in the multidrug ATP-binding cassette transporter BmrA.
Biochemistry: 2008, 47(8);2404-12
[PubMed:18215075] [WorldCat.org] [DOI] (P p)

Stéphanie Ravaud, Marie-Ange Do Cao, Marie Jidenko, Christine Ebel, Marc Le Maire, Jean-Michel Jault, Attilio Di Pietro, Richard Haser, Nushin Aghajari
The ABC transporter BmrA from Bacillus subtilis is a functional dimer when in a detergent-solubilized state.
Biochem J: 2006, 395(2);345-53
[PubMed:16405427] [WorldCat.org] [DOI] (I p)

Olivier Dalmas, Cédric Orelle, Anne-Emmanuelle Foucher, Christophe Geourjon, Serge Crouzy, Attilio Di Pietro, Jean-Michel Jault
The Q-loop disengages from the first intracellular loop during the catalytic cycle of the multidrug ABC transporter BmrA.
J Biol Chem: 2005, 280(44);36857-64
[PubMed:16107340] [WorldCat.org] [DOI] (P p)

Olivier Dalmas, Marie-Ange Do Cao, Miguel R Lugo, Frances J Sharom, Attilio Di Pietro, Jean-Michel Jault
Time-resolved fluorescence resonance energy transfer shows that the bacterial multidrug ABC half-transporter BmrA functions as a homodimer.
Biochemistry: 2005, 44(11);4312-21
[PubMed:15766260] [WorldCat.org] [DOI] (P p)

Emmanuelle Steinfels, Cédric Orelle, Jean-Raphaël Fantino, Olivier Dalmas, Jean-Louis Rigaud, François Denizot, Attilio Di Pietro, Jean-Michel Jault
Characterization of YvcC (BmrA), a multidrug ABC transporter constitutively expressed in Bacillus subtilis.
Biochemistry: 2004, 43(23);7491-502
[PubMed:15182191] [WorldCat.org] [DOI] (P p)

Cédric Orelle, Olivier Dalmas, Philippe Gros, Attilio Di Pietro, Jean-Michel Jault
The conserved glutamate residue adjacent to the Walker-B motif is the catalytic base for ATP hydrolysis in the ATP-binding cassette transporter BmrA.
J Biol Chem: 2003, 278(47);47002-8
[PubMed:12968023] [WorldCat.org] [DOI] (P p)

Emmanuelle Steinfels, Cédric Orelle, Olivier Dalmas, François Penin, Bruno Miroux, Attilio Di Pietro, Jean-Michel Jault
Highly efficient over-production in E. coli of YvcC, a multidrug-like ATP-binding cassette transporter from Bacillus subtilis.
Biochim Biophys Acta: 2002, 1565(1);1-5
[PubMed:12225846] [WorldCat.org] [DOI] (P p)

Mohamed Chami, Emmanuelle Steinfels, Cédric Orelle, Jean-Michel Jault, Attilio Di Pietro, Jean-Louis Rigaud, Sergio Marco
Three-dimensional structure by cryo-electron microscopy of YvcC, an homodimeric ATP-binding cassette transporter from Bacillus subtilis.
J Mol Biol: 2002, 315(5);1075-85
[PubMed:11827477] [WorldCat.org] [DOI] (P p)

Y Quentin, G Fichant, F Denizot
Inventory, assembly and analysis of Bacillus subtilis ABC transport systems.
J Mol Biol: 1999, 287(3);467-84
[PubMed:10092453] [WorldCat.org] [DOI] (P p)