ID BMR1_BACSU STANDARD; PRT; 389 AA. AC P33449; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 01-FEB-2005 (Rel. 46, Last annotation update) DE Multidrug resistance protein 1 (Multidrug-efflux transporter 1). GN Name=bmr; Synonyms=bmr1; OrderedLocusNames=BSU24010; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=168 / BD170; RX MEDLINE=91271277; PubMed=1675788; RA Neyfakh A.A., Bidnenko V.E., Chen L.B.; RT "Efflux-mediated multidrug resistance in Bacillus subtilis: RT similarities and dissimilarities with the mammalian system."; RL Proc. Natl. Acad. Sci. U.S.A. 88:4781-4785(1991). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=168 / Marburg; RX MEDLINE=95050642; PubMed=7961792; RA Ahmed M., Borsch C.M., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A.; RT "A protein that activates expression of a multidrug efflux transporter RT upon binding the transporter substrates."; RL J. Biol. Chem. 269:28506-28513(1994). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=168 / JH642; RX MEDLINE=97124195; PubMed=8969508; RA Mizuno M., Masuda S., Takemaru K.-I., Hosono S., Sato T., Takeuchi M., RA Kobayashi Y.; RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of RT the Bacillus subtilis genome containing the skin element and many RT sporulation genes."; RL Microbiology 142:3103-3111(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.K., Codani J.J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Dusterhoft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). CC -!- FUNCTION: Energy-dependent efflux pump responsible for decreased CC drug accumulation in multi-drug-resistant cells. Probably uses a CC transmembrane proton gradient as the energy source. Causes the CC efflux of a variety of toxic substances, including such CC structurally diverse compounds as ethidium bromide, rhodamine and CC acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, CC doxorubicin, and fluoroquinolone antibiotics. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/tetA CC family. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; M33768; AAA22277.1; -. DR EMBL; L25604; AAB81539.1; -. DR EMBL; D84432; BAA12601.1; -. DR EMBL; Z99116; CAB14332.1; -. DR PIR; A39705; A39705. DR SubtiList; BG10303; bmr. DR InterPro; IPR007114; MFS. DR InterPro; IPR005828; Sub_transporter. DR InterPro; IPR005829; Sug_transporter. DR InterPro; IPR001958; TCR_TetA. DR Pfam; PF00083; Sugar_tr; 1. DR PRINTS; PR01035; TCRTETA. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS00216; SUGAR_TRANSPORT_1; UNKNOWN_1. KW Antibiotic resistance; Complete proteome; Transmembrane; Transport. FT TRANSMEM 6 26 Potential. FT TRANSMEM 42 62 Potential. FT TRANSMEM 71 91 Potential. FT TRANSMEM 102 122 Potential. FT TRANSMEM 134 154 Potential. FT TRANSMEM 160 180 Potential. FT TRANSMEM 202 222 Potential. FT TRANSMEM 243 263 Potential. FT TRANSMEM 286 306 Potential. FT TRANSMEM 336 356 Potential. FT TRANSMEM 358 378 Potential. SQ SEQUENCE 389 AA; 42258 MW; 3A570DEE5836A127 CRC64; MEKKNITLTI LLTNLFIAFL GIGLVIPVTP TIMNELHLSG TAVGYMVACF AITQLIVSPI AGRWVDRFGR KIMIVIGLLF FSVSEFLFGI GKTVEMLFIS RMLGGISAPF IMPGVTAFIA DITTIKTRPK ALGYMSAAIS TGFIIGPGIG GFLAEVHSRL PFFFAAAFAL LAAILSILTL REPERNPENQ EIKGQKTGFK RIFAPMYFIA FLIILISSFG LASFESLFAL FVDHKFGFTA SDIAIMITGG AIVGAITQVV LFDRFTRWFG EIHLIRYSLI LSTSLVFLLT TVHSYVAILL VTVTVFVGFD LMRPAVTTYL SKIAGNEQGF AGGMNSMFTS IGNVFGPIIG GMLFDIDVNY PFYFATVTLA IGIALTIAWK APAHLKAST //