BmrA (B. subtilis 168)

B. subtilis multidrug resistance ATP-binding cassette (ABC) transporter ATP-binding protein (BmrA), also known as YvcC, is a multidrug ABC transporter that is constitutively expressed in B. subtilis.¹ It belongs to the ABC family and shares sequence homology to mammalian P-glycoprotein (P-gp) and LmrA from L. lactis. BmrA is also homologous to HorA, a multidrug ABC transporter from L. brevis, Q8Y3T6 and Q8NXS2, putative transporters from Gram-positive bacteria, and MsbA, a lipid A transporter from E. coli. BmrA transports Hoechst, doxorubicin, and 7-aminoactinomycin D in an ATP-dependent manner. The ATPase mutants BmrA^K380A and BmrA^K380R are completely devoid of transport activity. Mutations in the intergenic region preceding bmrA increase BmrA mRNA expression and bmrA promoter activity in B. subtilis, which confer resistance to the antibiotic cervimycin C.²

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1. Steinfels, E., Orelle, C., Fantino, J.-R., et al. Characterization of YvcC (BmrA), a multidrug ABC transporter constitutively expressed in Bacillus subtilis. Biochemistry 43(23), 7491-7502 (2004).

2. Krügel, U., Licht, A., Biedermann, G., et al. Cervimycin C resistance in Bacillus subtilis is due to a promoter up-mutation and increased mRNA stability of the constitutive ABC-transporter gene bmrA. FEMS Microbiol. Lett. 313(2), 155-163 (2010).