P39075 (BMRR_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Multidrug-efflux transporter 1 regulator

Gene names

Name:	bmrR
Synonyms:	bmr1R
Ordered Locus Names:	BSU24020

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	278 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Ligand	DNA-binding
Molecular function	Activator
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 278

278

Multidrug-efflux transporter 1 regulator

PRO_0000098109

Regions

Domain

5 – 75

71

HTH merR-type

DNA binding

8 – 27

20

H-T-H motif Potential

Secondary structure

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278

Helix Strand Turn

Details...

Beta strand

5 – 7

3

Helix

8 – 15

8

Helix

19 – 27

9

Beta strand

34 – 36

3

Turn

38 – 40

3

Beta strand

43 – 46

4

Helix

48 – 51

4

Helix

52 – 61

10

Helix

66 – 72

7

Helix

77 – 116

40

Beta strand

125 – 129

5

Beta strand

132 – 138

7

Turn

144 – 146

3

Helix

149 – 152

4

Helix

153 – 163

11

Beta strand

170 – 174

5

Helix

182 – 184

3

Beta strand

188 – 193

6

Beta strand

207 – 212

6

Beta strand

214 – 223

10

Helix

226 – 242

17

Beta strand

247 – 258

12

Beta strand

262 – 264

3

Beta strand

268 – 276

9

Sequences

	Sequence		Length	Mass (Da)
	P39075 [UniParc]. Last modified October 24, 2003. Version 3. Checksum: 184AEF0274991E73	FASTA	278	32,582
	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

References

	« Hide 'large scale' referencesShow '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: 7961792] [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: 8969508] [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: 9384377] [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: 10568751] [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: 10025401] [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: 11201751] [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.

PIR

E69595.

RefSeq

NP_390282.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BOW	X-ray	2.70	A	121-276	[»]
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	121-276	[»]
3D6Y	X-ray	2.70	A	1-274	[»]
3D6Z	X-ray	2.60	A	1-274	[»]
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	[»]

ProteinModelPortal

P39075.

SMR

P39075. Positions 3-277.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000003191; EBBACP00000003191; EBBACG00000003184.

GeneID

938676.

GenomeReviews

Gene locus BSU24020 in contig AL009126_GR.

KEGG

bsu:BSU24020.

PATRIC

18976631. VBIBacSub10457_2506.

Organism-specific databases

GenoList

BSU24020. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000001457.

HOGENOM

HBG534696.

OMA

RIISHTS.

ProtClustDB

CLSK748960.

Enzyme and pathway databases

BioCyc

BSUB:BSU24020-MONOMER.

Family and domain databases

InterPro

IPR010499. AraC_E-bd.
IPR009061. DNA-bd_dom_put.
IPR011256. Reg_factor_effector_bac.
IPR000551. Tscrpt_reg_HTH_MerR.
[Graphical view]

Pfam

PF06445. AraC_E_bind. 1 hit.
PF00376. MerR. 1 hit.
[Graphical view]

SMART

SM00422. HTH_MERR. 1 hit.
[Graphical view]

SUPFAM

SSF55136. Bac_reg_effector. 1 hit.
SSF46955. Putativ_DNA_bind. 1 hit.

PROSITE

PS00552. HTH_MERR_1. 1 hit.
PS50937. HTH_MERR_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BMRR_BACSU

Accession

Primary (citable) accession number: P39075

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 24, 2003
Last modified:	January 25, 2012
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program