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P39075

- BMRR_BACSU

UniProt

P39075 - BMRR_BACSU

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Protein
Multidrug-efflux transporter 1 regulator
Gene
bmrR, bmr1R, BSU24020
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 motif Reviewed prediction
Add
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
Complete GO annotation...

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 regulator
PRO_0000098109Add
BLAST

Proteomic databases

PaxDbiP39075.

Interactioni

Subunit structurei

Binds DNA as a homodimer.

Protein-protein interaction databases

DIPiDIP-59692N.
STRINGi224308.BSU24020.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP39075.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 7571HTH merR-type
Add
BLAST

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 116 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

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