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Protein

Multidrug transporter EmrE

Gene

emrE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multidrug transporter that expels positively charged hydrophobic drugs across the inner membrane of E.coli., thereby conferring resistance to a wide range of toxic compounds. The drug efflux is coupled to an influx of protons. Is involved in the resistance of E.coli cells to methyl viologen, ethidium bromide and acriflavine. Is also able to transport tetraphenylphosphonium (TPP+) and benzalkonium.4 Publications

Kineticsi

  1. KM=247 µM for methyl viologen1 Publication
  1. Vmax=1572 nmol/min/mg enzyme with methyl viologen as substrate1 Publication

pH dependencei

Optimum pH is 8-8.5. Transport activity occurs from pH 7.5 to 9.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei4Required for proper coupling between the substrate transport and the proton gradient1
Sitei14Essential for translocation and for substrate and proton binding1
Sitei40Involved in substrate binding1
Sitei60Involved in substrate binding1
Sitei63Involved in substrate binding1

GO - Molecular functioni

  • amino-acid betaine transmembrane transporter activity Source: EcoCyc
  • antiporter activity Source: EcoliWiki
  • choline transmembrane transporter activity Source: EcoCyc
  • drug:proton antiporter activity Source: EcoCyc
  • transmembrane transporter activity Source: CACAO

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • choline transport Source: EcoCyc
  • glycine betaine transport Source: EcoCyc
  • response to drug Source: EcoliWiki
  • response to osmotic stress Source: EcoCyc
  • transport Source: EcoliWiki
  • xenobiotic metabolic process Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

Antiport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EMRE-MONOMER.
ECOL316407:JW0531-MONOMER.
MetaCyc:EMRE-MONOMER.
SABIO-RKP23895.

Protein family/group databases

TCDBi2.A.7.1.3. the drug/metabolite transporter (dmt) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Multidrug transporter EmrE
Alternative name(s):
Efflux-multidrug resistance protein EmrE
Ethidium resistance protein
Methyl viologen resistance protein C
Gene namesi
Name:emrE
Synonyms:eb, mvrC
Ordered Locus Names:b0543, JW0531
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10629. emrE.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 3Cytoplasmic3
Transmembranei4 – 21Helical; Name=1Add BLAST18
Topological domaini22 – 33PeriplasmicAdd BLAST12
Transmembranei34 – 52Helical; Name=2Add BLAST19
Topological domaini53 – 57Cytoplasmic5
Transmembranei58 – 81Helical; Name=3Add BLAST24
Topological domaini82 – 84Periplasmic3
Transmembranei85 – 105Helical; Name=4Add BLAST21
Topological domaini106 – 110Cytoplasmic5

GO - Cellular componenti

  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: EcoCyc
  • membrane Source: EcoliWiki
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4Y → C: Still binds substrate. No transport activity in the presence of a proton gradient, but still transports substrate in the absence of a proton gradient. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi4Y → F or W: No effect on resistance to toxicants. 1 Publication1
Mutagenesisi6Y → C, F or L: No effect on resistance to toxicants. 1 Publication1
Mutagenesisi7L → C: No substrate binding. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi10A → C: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi11I → C: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi14E → C: No substrate binding. No transport activity. Resistance to toxicants is abolished. 2 Publications1
Mutagenesisi14E → D: Still binds substrate. No transport activity in the presence of a proton gradient, but still transports substrate in the absence of a proton gradient. Resistance to toxicants is abolished. 2 Publications1
Mutagenesisi17G → C: No substrate binding. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi18T → C: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi40Y → C, F, L, M, S, T or V: Modifies substrate specificity. 1 Publication1
Mutagenesisi53Y → C: No effect on resistance to toxicants. 1 Publication1
Mutagenesisi60Y → C or F: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi63W → C or Y: No transport activity. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi63W → F: Still binds substrate, with two-fold reduction in substrate affinity. Resistance to toxicants is abolished. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001080741 – 110Multidrug transporter EmrEAdd BLAST110

Proteomic databases

PaxDbiP23895.
PRIDEiP23895.

Interactioni

Subunit structurei

Homodimer; parallel. May also form dimer of homodimers. Binds substrate at the dimerization interface.5 Publications

Protein-protein interaction databases

BioGridi4259366. 101 interactors.
DIPiDIP-9505N.
STRINGi511145.b0543.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I68electron microscopy-A/B1-110[»]
3B5DX-ray3.80A/B1-110[»]
3B61X-ray4.50A/B/C/D/E/F/G/H1-110[»]
3B62X-ray4.40A/B/C/D1-110[»]
ProteinModelPortaliP23895.
SMRiP23895.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23895.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410814C. Bacteria.
COG2076. LUCA.
HOGENOMiHOG000268006.
InParanoidiP23895.
KOiK03297.
OMAiYAIAFWM.
PhylomeDBiP23895.

Family and domain databases

InterProiIPR000390. Small_multidrug_res.
[Graphical view]
PfamiPF00893. Multi_Drug_Res. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23895-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPYIYLGGA ILAEVIGTTL MKFSEGFTRL WPSVGTIICY CASFWLLAQT
60 70 80 90 100
LAYIPTGIAY AIWSGVGIVL ISLLSWGFFG QRLDLPAIIG MMLICAGVLI
110
INLLSRSTPH
Length:110
Mass (Da):11,958
Last modified:November 1, 1991 - v1
Checksum:i775153FC47D6AE3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11877 Genomic DNA. Translation: CAA77936.1.
M62732 Genomic DNA. Translation: AAA24190.1.
U82598 Genomic DNA. Translation: AAB40740.1.
U00096 Genomic DNA. Translation: AAC73644.1.
AP009048 Genomic DNA. Translation: BAE76318.1.
PIRiJN0329.
RefSeqiNP_415075.1. NC_000913.3.
WP_001070439.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73644; AAC73644; b0543.
BAE76318; BAE76318; BAE76318.
GeneIDi948442.
KEGGiecj:JW0531.
eco:b0543.
PATRICi32116248. VBIEscCol129921_0564.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11877 Genomic DNA. Translation: CAA77936.1.
M62732 Genomic DNA. Translation: AAA24190.1.
U82598 Genomic DNA. Translation: AAB40740.1.
U00096 Genomic DNA. Translation: AAC73644.1.
AP009048 Genomic DNA. Translation: BAE76318.1.
PIRiJN0329.
RefSeqiNP_415075.1. NC_000913.3.
WP_001070439.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I68electron microscopy-A/B1-110[»]
3B5DX-ray3.80A/B1-110[»]
3B61X-ray4.50A/B/C/D/E/F/G/H1-110[»]
3B62X-ray4.40A/B/C/D1-110[»]
ProteinModelPortaliP23895.
SMRiP23895.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259366. 101 interactors.
DIPiDIP-9505N.
STRINGi511145.b0543.

Protein family/group databases

TCDBi2.A.7.1.3. the drug/metabolite transporter (dmt) superfamily.

Proteomic databases

PaxDbiP23895.
PRIDEiP23895.

Protocols and materials databases

DNASUi948442.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73644; AAC73644; b0543.
BAE76318; BAE76318; BAE76318.
GeneIDi948442.
KEGGiecj:JW0531.
eco:b0543.
PATRICi32116248. VBIEscCol129921_0564.

Organism-specific databases

EchoBASEiEB0623.
EcoGeneiEG10629. emrE.

Phylogenomic databases

eggNOGiENOG410814C. Bacteria.
COG2076. LUCA.
HOGENOMiHOG000268006.
InParanoidiP23895.
KOiK03297.
OMAiYAIAFWM.
PhylomeDBiP23895.

Enzyme and pathway databases

BioCyciEcoCyc:EMRE-MONOMER.
ECOL316407:JW0531-MONOMER.
MetaCyc:EMRE-MONOMER.
SABIO-RKP23895.

Miscellaneous databases

EvolutionaryTraceiP23895.
PROiP23895.

Family and domain databases

InterProiIPR000390. Small_multidrug_res.
[Graphical view]
PfamiPF00893. Multi_Drug_Res. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEMRE_ECOLI
AccessioniPrimary (citable) accession number: P23895
Secondary accession number(s): Q2MBN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 2, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Encoded by the cryptic lambdoid prophage DLP12.

Caution

EM structures show an asymmetric dimer with the monomers in an antiparallel orientation, in contradiction with biochemical data and cross-linking studies, which demonstrated a parallel arrangement. Until now, EmrE with a parallel orientation is the only one to be shown to be fully functional.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.