The multidrug efflux transporter of Bacillus subtilis is a structural and functional homolog of the Staphylococcus NorA protein

Antimicrob Agents Chemother. 1992 Feb;36(2):484-5. doi: 10.1128/AAC.36.2.484.

Abstract

The Bacillus subtilis multidrug efflux transporter Bmr demonstrates 44% amino acid sequence identity with a product of the Staphylococcus aureus gene norA, which is responsible for clinically relevant resistance to fluoroquinolones. We show here that overexpression of bmr in B. subtilis provides strong resistance to fluoroquinolones that can be reversed by reserpine, an inhibitor of Bmr.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / genetics
  • Bacillus subtilis / metabolism*
  • Bacterial Proteins / analysis
  • Bacterial Proteins / metabolism*
  • Carrier Proteins*
  • Membrane Transport Proteins*
  • Molecular Sequence Data
  • Multidrug Resistance-Associated Proteins
  • Reserpine / pharmacology
  • Sequence Homology, Nucleic Acid
  • Staphylococcus aureus / genetics
  • Staphylococcus aureus / metabolism*

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Membrane Transport Proteins
  • Multidrug Resistance-Associated Proteins
  • NorA protein, Staphylococcus
  • Bmr protein, Bacillus subtilis
  • Reserpine

Associated data

  • GENBANK/M33768