BMRR_BACSU
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 03-AUG-2022, entry version 148.
DE RecName: Full=Multidrug-efflux transporter 1 regulator;
GN Name=bmrR; Synonyms=bmr1R; OrderedLocusNames=BSU24020;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; 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 / NCIMB
RC 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};
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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 SMR; P39075; -.
DR DIP; DIP-59692N; -.
DR STRING; 224308.BSU24020; -.
DR PaxDb; P39075; -.
DR PRIDE; P39075; -.
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 OMA; VEMKIRI; -.
DR PhylomeDB; P39075; -.
DR BioCyc; BSUB:BSU24020-MON; -.
DR EvolutionaryTrace; P39075; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.20.80.10; -; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR029442; GyrI-like.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR InterPro; IPR011256; Reg_factor_effector_dom_sf.
DR Pfam; PF06445; GyrI-like; 1.
DR Pfam; PF13411; MerR_1; 1.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF55136; SSF55136; 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
