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P39075

- BMRR_BACSU

UniProt

P39075 - BMRR_BACSU

Protein

Multidrug-efflux transporter 1 regulator

Gene

bmrR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 3 (24 Oct 2003)
      Previous versions | rss
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    Functioni

    Activates transcription of the bmr gene in response to structurally dissimilar drugs. Binds rhodamine as an inducer.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi8 – 2720H-T-H motifPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU24020-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Multidrug-efflux transporter 1 regulator
    Gene namesi
    Name:bmrR
    Synonyms:bmr1R
    Ordered Locus Names:BSU24020
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU24020. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 278278Multidrug-efflux transporter 1 regulatorPRO_0000098109Add
    BLAST

    Proteomic databases

    PaxDbiP39075.

    Interactioni

    Subunit structurei

    Binds DNA as a homodimer.

    Protein-protein interaction databases

    DIPiDIP-59692N.
    STRINGi224308.BSU24020.

    Structurei

    Secondary structure

    1
    278
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Helixi8 – 158
    Helixi19 – 279
    Beta strandi34 – 363
    Turni38 – 403
    Beta strandi43 – 464
    Helixi48 – 514
    Helixi52 – 6110
    Helixi66 – 727
    Helixi77 – 11640
    Beta strandi119 – 1213
    Beta strandi125 – 1295
    Beta strandi132 – 1387
    Turni144 – 1463
    Helixi149 – 1524
    Helixi153 – 16311
    Beta strandi170 – 1745
    Helixi182 – 1843
    Beta strandi188 – 1936
    Beta strandi207 – 2126
    Beta strandi214 – 22310
    Helixi226 – 24217
    Beta strandi247 – 25812
    Beta strandi262 – 2643
    Beta strandi268 – 2769

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BOWX-ray2.70A121-278[»]
    1EXIX-ray3.12A1-278[»]
    1EXJX-ray3.00A1-278[»]
    1R8EX-ray2.40A1-278[»]
    2BOWX-ray2.80A121-278[»]
    3D6YX-ray2.70A1-278[»]
    3D6ZX-ray2.60A1-278[»]
    3D70X-ray2.80A2-278[»]
    3D71X-ray2.80A1-276[»]
    3IAOX-ray2.80A1-278[»]
    3Q1MX-ray3.20A1-276[»]
    3Q2YX-ray2.95A1-276[»]
    3Q3DX-ray2.79A1-276[»]
    3Q5PX-ray2.94A1-276[»]
    3Q5RX-ray3.05A1-276[»]
    3Q5SX-ray3.10A1-276[»]
    ProteinModelPortaliP39075.
    SMRiP39075. Positions 3-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39075.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 7571HTH merR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 HTH merR-type DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0789.
    HOGENOMiHOG000050346.
    OMAiVEMKIRI.
    OrthoDBiEOG6CK7SS.
    PhylomeDBiP39075.

    Family and domain databases

    Gene3Di3.20.80.10. 1 hit.
    InterProiIPR009061. DNA-bd_dom_put.
    IPR029442. GyrI-like.
    IPR000551. MerR-type_HTH_dom.
    IPR011256. Reg_factor_effector_dom.
    [Graphical view]
    PfamiPF06445. GyrI-like. 1 hit.
    PF00376. MerR. 1 hit.
    [Graphical view]
    SMARTiSM00422. HTH_MERR. 1 hit.
    [Graphical view]
    SUPFAMiSSF46955. SSF46955. 1 hit.
    SSF55136. SSF55136. 1 hit.
    PROSITEiPS00552. HTH_MERR_1. 1 hit.
    PS50937. HTH_MERR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39075-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKESYYSIGE VSKLANVSIK ALRYYDKIDL FKPAYVDPDT SYRYYTDSQL    50
    IHLDLIKSLK YIGTPLEEMK KAQDLEMEEL FAFYTEQERQ IREKLDFLSA 100
    LEQTISLVKK RMKRQMEYPA LGEVFVLDEE EIRIIQTEAE GIGPENVLNA 150
    SYSKLKKFIE SADGFTNNSY GATFSFQPYT SIDEMTYRHI FTPVLTNKQI 200
    SSITPDMEIT TIPKGRYACI AYNFSPEHYF LNLQKLIKYI ADRQLTVVSD 250
    VYELIIPIHY SPKKQEEYRV EMKIRIAE 278
    Length:278
    Mass (Da):32,582
    Last modified:October 24, 2003 - v3
    Checksum:i184AEF0274991E73
    GO

    Sequence cautioni

    The sequence BAA23495.1 differs from that shown. Reason: Frameshift at positions 74 and 120.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25604 Genomic DNA. Translation: AAB81540.2.
    D84432 Genomic DNA. Translation: BAA23495.1. Sequence problems.
    AL009126 Genomic DNA. Translation: CAB14333.2.
    PIRiE69595.
    RefSeqiNP_390282.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB14333; CAB14333; BSU24020.
    GeneIDi938676.
    KEGGibsu:BSU24020.
    PATRICi18976631. VBIBacSub10457_2506.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25604 Genomic DNA. Translation: AAB81540.2 .
    D84432 Genomic DNA. Translation: BAA23495.1 . Sequence problems.
    AL009126 Genomic DNA. Translation: CAB14333.2 .
    PIRi E69595.
    RefSeqi NP_390282.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BOW X-ray 2.70 A 121-278 [» ]
    1EXI X-ray 3.12 A 1-278 [» ]
    1EXJ X-ray 3.00 A 1-278 [» ]
    1R8E X-ray 2.40 A 1-278 [» ]
    2BOW X-ray 2.80 A 121-278 [» ]
    3D6Y X-ray 2.70 A 1-278 [» ]
    3D6Z X-ray 2.60 A 1-278 [» ]
    3D70 X-ray 2.80 A 2-278 [» ]
    3D71 X-ray 2.80 A 1-276 [» ]
    3IAO X-ray 2.80 A 1-278 [» ]
    3Q1M X-ray 3.20 A 1-276 [» ]
    3Q2Y X-ray 2.95 A 1-276 [» ]
    3Q3D X-ray 2.79 A 1-276 [» ]
    3Q5P X-ray 2.94 A 1-276 [» ]
    3Q5R X-ray 3.05 A 1-276 [» ]
    3Q5S X-ray 3.10 A 1-276 [» ]
    ProteinModelPortali P39075.
    SMRi P39075. Positions 3-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59692N.
    STRINGi 224308.BSU24020.

    Proteomic databases

    PaxDbi P39075.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14333 ; CAB14333 ; BSU24020 .
    GeneIDi 938676.
    KEGGi bsu:BSU24020.
    PATRICi 18976631. VBIBacSub10457_2506.

    Organism-specific databases

    GenoListi BSU24020. [Micado ]

    Phylogenomic databases

    eggNOGi COG0789.
    HOGENOMi HOG000050346.
    OMAi VEMKIRI.
    OrthoDBi EOG6CK7SS.
    PhylomeDBi P39075.

    Enzyme and pathway databases

    BioCyci BSUB:BSU24020-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P39075.

    Family and domain databases

    Gene3Di 3.20.80.10. 1 hit.
    InterProi IPR009061. DNA-bd_dom_put.
    IPR029442. GyrI-like.
    IPR000551. MerR-type_HTH_dom.
    IPR011256. Reg_factor_effector_dom.
    [Graphical view ]
    Pfami PF06445. GyrI-like. 1 hit.
    PF00376. MerR. 1 hit.
    [Graphical view ]
    SMARTi SM00422. HTH_MERR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46955. SSF46955. 1 hit.
    SSF55136. SSF55136. 1 hit.
    PROSITEi PS00552. HTH_MERR_1. 1 hit.
    PS50937. HTH_MERR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates."
      Ahmed M., Borsch C.M., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A.
      J. Biol. Chem. 269:28506-28513(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
    2. Neyfakh A.A.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
      Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
      Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / JH642.
    4. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    5. "Detecting and analyzing DNA sequencing errors: toward a higher quality of the Bacillus subtilis genome sequence."
      Medigue C., Rose M., Viari A., Danchin A.
      Genome Res. 9:1116-1127(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    6. "Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter."
      Zheleznova E.E., Markham P.N., Neyfakh A.A., Brennan R.G.
      Cell 96:353-362(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 120-228.
    7. "Crystal structure of the transcription activator BmrR bound to DNA and a drug."
      Heldwein E.E., Brennan R.G.
      Nature 409:378-382(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS).

    Entry informationi

    Entry nameiBMRR_BACSU
    AccessioniPrimary (citable) accession number: P39075
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: October 24, 2003
    Last modified: October 1, 2014
    This is version 117 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3