Difference between revisions of "BmrA"

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[[Category:Protein-coding genes]]

Revision as of 12:51, 21 July 2009

  • Description: multidrug ABC transporter (ATP-binding protein)

Gene name bmrA
Synonyms yvcC
Essential no
Product multidrug ABC transporter (ATP-binding protein)
Function multiple antibiotic resistance
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



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:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

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

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • 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

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)

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)