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Protein

Multidrug-efflux transporter 1 regulator

Gene

bmrR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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 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
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 Componenti: 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 – 73Combined sources
Helixi8 – 158Combined sources
Helixi19 – 279Combined sources
Beta strandi34 – 363Combined sources
Turni38 – 403Combined sources
Beta strandi43 – 464Combined sources
Helixi48 – 514Combined sources
Helixi52 – 6110Combined sources
Helixi66 – 727Combined sources
Helixi77 – 11640Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi125 – 1295Combined sources
Beta strandi132 – 1387Combined sources
Turni144 – 1463Combined sources
Helixi149 – 1524Combined sources
Helixi153 – 16311Combined sources
Beta strandi170 – 1745Combined sources
Helixi182 – 1843Combined sources
Beta strandi188 – 1936Combined sources
Beta strandi207 – 2126Combined sources
Beta strandi214 – 22310Combined sources
Helixi226 – 24217Combined sources
Beta strandi247 – 25812Combined sources
Beta strandi262 – 2643Combined sources
Beta strandi268 – 2769Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MKESYYSIGE VSKLANVSIK ALRYYDKIDL FKPAYVDPDT SYRYYTDSQL
60 70 80 90 100
IHLDLIKSLK YIGTPLEEMK KAQDLEMEEL FAFYTEQERQ IREKLDFLSA
110 120 130 140 150
LEQTISLVKK RMKRQMEYPA LGEVFVLDEE EIRIIQTEAE GIGPENVLNA
160 170 180 190 200
SYSKLKKFIE SADGFTNNSY GATFSFQPYT SIDEMTYRHI FTPVLTNKQI
210 220 230 240 250
SSITPDMEIT TIPKGRYACI AYNFSPEHYF LNLQKLIKYI ADRQLTVVSD
260 270
VYELIIPIHY SPKKQEEYRV EMKIRIAE
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

DIPiDIP-59692N.
STRINGi224308.BSU24020.

Proteomic databases

PaxDbiP39075.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU24020. [Micado]

Phylogenomic databases

eggNOGiCOG0789.
HOGENOMiHOG000050346.
OMAiVEMKIRI.
OrthoDBiEOG6CK7SS.
PhylomeDBiP39075.

Enzyme and pathway databases

BioCyciBSUB:BSU24020-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP39075.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 119 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.