Difference between revisions of "BmrA"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yvcD]]'', ''[[yvzA]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yvcD]]'', ''[[yvzA]]''
 
|-
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU34820 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU34820 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU34820 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU34820 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU34820 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU34820 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:yvcC_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:yvcC_context.gif]]

Revision as of 11:22, 14 May 2013

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
Sequences Protein DNA DNA_with_flanks
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)