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P39075 (BMRR_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multidrug-efflux transporter 1 regulator
Gene names
Name:bmrR
Synonyms:bmr1R
Ordered Locus Names:BSU24020
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Binds DNA as a homodimer.

Sequence similarities

Contains 1 HTH merR-type DNA-binding domain.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   LigandDNA-binding
   Molecular functionActivator
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 278278Multidrug-efflux transporter 1 regulator
PRO_0000098109

Regions

Domain5 – 7571HTH merR-type
DNA binding8 – 2720H-T-H motif Potential

Secondary structure

................................................ 278
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39075 [UniParc].

Last modified October 24, 2003. Version 3.
Checksum: 184AEF0274991E73

FASTA27832,582
        10         20         30         40         50         60 
MKESYYSIGE VSKLANVSIK ALRYYDKIDL FKPAYVDPDT SYRYYTDSQL IHLDLIKSLK 

        70         80         90        100        110        120 
YIGTPLEEMK KAQDLEMEEL FAFYTEQERQ IREKLDFLSA LEQTISLVKK RMKRQMEYPA 

       130        140        150        160        170        180 
LGEVFVLDEE EIRIIQTEAE GIGPENVLNA SYSKLKKFIE SADGFTNNSY GATFSFQPYT 

       190        200        210        220        230        240 
SIDEMTYRHI FTPVLTNKQI SSITPDMEIT TIPKGRYACI AYNFSPEHYF LNLQKLIKYI 

       250        260        270 
ADRQLTVVSD VYELIIPIHY SPKKQEEYRV EMKIRIAE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L25604 Genomic DNA. Translation: AAB81540.2.
D84432 Genomic DNA. Translation: BAA23495.1. Sequence problems.
AL009126 Genomic DNA. Translation: CAB14333.2.
PIRE69595.
RefSeqNP_390282.2. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP39075.
SMRP39075. Positions 3-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59692N.
STRING224308.BSU24020.

Proteomic databases

PaxDbP39075.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14333; CAB14333; BSU24020.
GeneID938676.
KEGGbsu:BSU24020.
PATRIC18976631. VBIBacSub10457_2506.

Organism-specific databases

GenoListBSU24020. [Micado]

Phylogenomic databases

eggNOGCOG0789.
HOGENOMHOG000050346.
OMAVEMKIRI.
OrthoDBEOG6CK7SS.
PhylomeDBP39075.

Enzyme and pathway databases

BioCycBSUB:BSU24020-MONOMER.

Family and domain databases

Gene3D3.20.80.10. 1 hit.
InterProIPR009061. DNA-bd_dom_put.
IPR029442. GyrI-like.
IPR000551. MerR-type_HTH_dom.
IPR011256. Reg_factor_effector_dom.
[Graphical view]
PfamPF06445. GyrI-like. 1 hit.
PF00376. MerR. 1 hit.
[Graphical view]
SMARTSM00422. HTH_MERR. 1 hit.
[Graphical view]
SUPFAMSSF46955. SSF46955. 1 hit.
SSF55136. SSF55136. 1 hit.
PROSITEPS00552. HTH_MERR_1. 1 hit.
PS50937. HTH_MERR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP39075.

Entry information

Entry nameBMRR_BACSU
AccessionPrimary (citable) accession number: P39075
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList