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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)DescriptionActionsGraphical viewLength
DNA bindingi8 – 27H-T-H motifPROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000981091 – 278Multidrug-efflux transporter 1 regulatorAdd BLAST278

Proteomic databases

PaxDbiP39075.
PRIDEiP39075.

Interactioni

Subunit structurei

Binds DNA as a homodimer.

Protein-protein interaction databases

DIPiDIP-59692N.
STRINGi224308.Bsubs1_010100013176.

Structurei

Secondary structure

1278
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Helixi8 – 15Combined sources8
Helixi19 – 27Combined sources9
Beta strandi34 – 36Combined sources3
Turni38 – 40Combined sources3
Beta strandi43 – 46Combined sources4
Helixi48 – 51Combined sources4
Helixi52 – 61Combined sources10
Helixi66 – 72Combined sources7
Helixi77 – 116Combined sources40
Beta strandi119 – 121Combined sources3
Beta strandi125 – 129Combined sources5
Beta strandi132 – 138Combined sources7
Turni144 – 146Combined sources3
Helixi149 – 152Combined sources4
Helixi153 – 163Combined sources11
Beta strandi170 – 174Combined sources5
Helixi182 – 184Combined sources3
Beta strandi188 – 193Combined sources6
Beta strandi207 – 212Combined sources6
Beta strandi214 – 223Combined sources10
Helixi226 – 242Combined sources17
Beta strandi247 – 258Combined sources12
Beta strandi262 – 264Combined sources3
Beta strandi268 – 276Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39075.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 75HTH merR-typePROSITE-ProRule annotationAdd BLAST71

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0789. LUCA.
COG4978. LUCA.
HOGENOMiHOG000050346.
KOiK19575.
OMAiVEMKIRI.
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.
PF13411. MerR_1. 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 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.
WP_003230325.1. NZ_JNCM01000036.1.

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.
WP_003230325.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59692N.
STRINGi224308.Bsubs1_010100013176.

Proteomic databases

PaxDbiP39075.
PRIDEiP39075.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0789. LUCA.
COG4978. LUCA.
HOGENOMiHOG000050346.
KOiK19575.
OMAiVEMKIRI.
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.
PF13411. MerR_1. 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...

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: November 2, 2016
This is version 128 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

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 one 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.