ID BMRR_BACSU Reviewed; 278 AA. AC P39075; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 24-OCT-2003, sequence version 3. DT 27-MAR-2024, entry version 157. DE RecName: Full=Multidrug-efflux transporter 1 regulator; GN Name=bmrR; Synonyms=bmr1R; OrderedLocusNames=BSU24020; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / RC NCIMB 3610 / NRRL NRS-744 / VKM B-501; RX PubMed=7961792; DOI=10.1016/s0021-9258(18)46956-6; 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 upon RT binding the transporter substrates."; RL J. Biol. Chem. 269:28506-28513(1994). RN [2] RP SEQUENCE REVISION. RA Neyfakh A.A.; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / JH642; RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103; RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., RA Kobayashi Y.; RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the RT Bacillus subtilis genome containing the skin element and many sporulation RT genes."; RL Microbiology 142:3103-3111(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., 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., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., 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). RN [5] RP SEQUENCE REVISION. RX PubMed=10568751; DOI=10.1101/gr.9.11.1116; RA Medigue C., Rose M., Viari A., Danchin A.; RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of RT the Bacillus subtilis genome sequence."; RL Genome Res. 9:1116-1127(1999). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 120-228. RX PubMed=10025401; DOI=10.1016/s0092-8674(00)80548-6; RA Zheleznova E.E., Markham P.N., Neyfakh A.A., Brennan R.G.; RT "Structural basis of multidrug recognition by BmrR, a transcription RT activator of a multidrug transporter."; RL Cell 96:353-362(1999). RN [7] RP X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS). RX PubMed=11201751; DOI=10.1038/35053138; RA Heldwein E.E., Brennan R.G.; RT "Crystal structure of the transcription activator BmrR bound to DNA and a RT drug."; RL Nature 409:378-382(2001). CC -!- FUNCTION: Activates transcription of the bmr gene in response to CC structurally dissimilar drugs. Binds rhodamine as an inducer. CC -!- SUBUNIT: Binds DNA as a homodimer. CC -!- SEQUENCE CAUTION: CC Sequence=BAA23495.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L25604; AAB81540.2; -; Genomic_DNA. DR EMBL; D84432; BAA23495.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL009126; CAB14333.2; -; Genomic_DNA. DR PIR; E69595; E69595. DR RefSeq; NP_390282.2; NC_000964.3. DR RefSeq; WP_003230325.1; NZ_JNCM01000036.1. DR PDB; 1BOW; X-ray; 2.70 A; A=121-278. DR PDB; 1EXI; X-ray; 3.12 A; A=1-278. DR PDB; 1EXJ; X-ray; 3.00 A; A=1-278. DR PDB; 1R8E; X-ray; 2.40 A; A=1-278. DR PDB; 2BOW; X-ray; 2.80 A; A=121-278. DR PDB; 3D6Y; X-ray; 2.70 A; A=1-278. DR PDB; 3D6Z; X-ray; 2.60 A; A=1-278. DR PDB; 3D70; X-ray; 2.80 A; A=2-278. DR PDB; 3D71; X-ray; 2.80 A; A=1-276. DR PDB; 3IAO; X-ray; 2.80 A; A=1-278. DR PDB; 3Q1M; X-ray; 3.20 A; A=1-276. DR PDB; 3Q2Y; X-ray; 2.95 A; A=1-276. DR PDB; 3Q3D; X-ray; 2.79 A; A=1-276. DR PDB; 3Q5P; X-ray; 2.94 A; A=1-276. DR PDB; 3Q5R; X-ray; 3.05 A; A=1-276. DR PDB; 3Q5S; X-ray; 3.10 A; A=1-276. DR PDB; 7CKQ; EM; 4.40 A; G/I=1-278. DR PDBsum; 1BOW; -. DR PDBsum; 1EXI; -. DR PDBsum; 1EXJ; -. DR PDBsum; 1R8E; -. DR PDBsum; 2BOW; -. DR PDBsum; 3D6Y; -. DR PDBsum; 3D6Z; -. DR PDBsum; 3D70; -. DR PDBsum; 3D71; -. DR PDBsum; 3IAO; -. DR PDBsum; 3Q1M; -. DR PDBsum; 3Q2Y; -. DR PDBsum; 3Q3D; -. DR PDBsum; 3Q5P; -. DR PDBsum; 3Q5R; -. DR PDBsum; 3Q5S; -. DR PDBsum; 7CKQ; -. DR AlphaFoldDB; P39075; -. DR EMDB; EMD-30390; -. DR SMR; P39075; -. DR DIP; DIP-59692N; -. DR STRING; 224308.BSU24020; -. DR PaxDb; 224308-BSU24020; -. DR EnsemblBacteria; CAB14333; CAB14333; BSU_24020. DR GeneID; 938676; -. DR KEGG; bsu:BSU24020; -. DR PATRIC; fig|224308.179.peg.2616; -. DR eggNOG; COG0789; Bacteria. DR eggNOG; COG4978; Bacteria. DR InParanoid; P39075; -. DR OrthoDB; 9773308at2; -. DR PhylomeDB; P39075; -. DR BioCyc; BSUB:BSU24020-MONOMER; -. DR EvolutionaryTrace; P39075; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro. DR CDD; cd01107; HTH_BmrR; 1. DR Gene3D; 1.10.1660.10; -; 1. DR Gene3D; 3.20.80.10; Regulatory factor, effector binding domain; 1. DR Gene3D; 1.20.5.490; Single helix bin; 1. DR InterPro; IPR009061; DNA-bd_dom_put_sf. DR InterPro; IPR029442; GyrI-like. DR InterPro; IPR000551; MerR-type_HTH_dom. DR InterPro; IPR047057; MerR_fam. DR InterPro; IPR011256; Reg_factor_effector_dom_sf. DR PANTHER; PTHR30204:SF87; MULTIDRUG-EFFLUX TRANSPORTER 1 REGULATOR; 1. DR PANTHER; PTHR30204; REDOX-CYCLING DRUG-SENSING TRANSCRIPTIONAL ACTIVATOR SOXR; 1. DR Pfam; PF06445; GyrI-like; 1. DR Pfam; PF13411; MerR_1; 1. DR SMART; SM00422; HTH_MERR; 1. DR SUPFAM; SSF55136; Probable bacterial effector-binding domain; 1. DR SUPFAM; SSF46955; Putative DNA-binding domain; 1. DR PROSITE; PS00552; HTH_MERR_1; 1. DR PROSITE; PS50937; HTH_MERR_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..278 FT /note="Multidrug-efflux transporter 1 regulator" FT /id="PRO_0000098109" FT DOMAIN 5..75 FT /note="HTH merR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254" FT DNA_BIND 8..27 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254" FT STRAND 5..7 FT /evidence="ECO:0007829|PDB:1R8E" FT HELIX 8..15 FT /evidence="ECO:0007829|PDB:1R8E" FT HELIX 19..27 FT /evidence="ECO:0007829|PDB:1R8E" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:1R8E" FT TURN 38..40 FT /evidence="ECO:0007829|PDB:1R8E" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:1R8E" FT HELIX 48..51 FT /evidence="ECO:0007829|PDB:1R8E" FT HELIX 52..61 FT /evidence="ECO:0007829|PDB:1R8E" FT HELIX 66..72 FT /evidence="ECO:0007829|PDB:1R8E" FT HELIX 77..116 FT /evidence="ECO:0007829|PDB:1R8E" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:1EXJ" FT STRAND 125..129 FT /evidence="ECO:0007829|PDB:1R8E" FT STRAND 132..138 FT /evidence="ECO:0007829|PDB:1R8E" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:1R8E" FT HELIX 149..152 FT /evidence="ECO:0007829|PDB:1R8E" FT HELIX 153..163 FT /evidence="ECO:0007829|PDB:1R8E" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:1R8E" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:1R8E" FT STRAND 188..193 FT /evidence="ECO:0007829|PDB:1R8E" FT STRAND 207..212 FT /evidence="ECO:0007829|PDB:1R8E" FT STRAND 214..223 FT /evidence="ECO:0007829|PDB:1R8E" FT HELIX 226..242 FT /evidence="ECO:0007829|PDB:1R8E" FT STRAND 247..258 FT /evidence="ECO:0007829|PDB:1R8E" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:1R8E" FT STRAND 268..276 FT /evidence="ECO:0007829|PDB:1R8E" SQ SEQUENCE 278 AA; 32582 MW; 184AEF0274991E73 CRC64; MKESYYSIGE VSKLANVSIK ALRYYDKIDL FKPAYVDPDT SYRYYTDSQL IHLDLIKSLK YIGTPLEEMK KAQDLEMEEL FAFYTEQERQ IREKLDFLSA LEQTISLVKK RMKRQMEYPA LGEVFVLDEE EIRIIQTEAE GIGPENVLNA SYSKLKKFIE SADGFTNNSY GATFSFQPYT SIDEMTYRHI FTPVLTNKQI SSITPDMEIT TIPKGRYACI AYNFSPEHYF LNLQKLIKYI ADRQLTVVSD VYELIIPIHY SPKKQEEYRV EMKIRIAE //