BmrA

• 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 This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU34820

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:

• Localization: membrane PubMed

Database entries

• Structure:

• UniProt: O06967

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

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)

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)