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P23895

- EMRE_ECOLI

UniProt

P23895 - EMRE_ECOLI

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Protein

Multidrug transporter EmrE

Gene
emrE, eb, mvrC, b0543, JW0531
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Vmax=1572 nmol/min/mg enzyme with methyl viologen as substrate

pH dependencei

Optimum pH is 8-8.5. Transport activity occurs from pH 7.5 to 9.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei4 – 41Required for proper coupling between the substrate transport and the proton gradient
Sitei14 – 141Essential for translocation and for substrate and proton binding
Sitei40 – 401Involved in substrate binding
Sitei60 – 601Involved in substrate binding
Sitei63 – 631Involved in substrate binding

GO - Molecular functioni

  1. amino-acid betaine transmembrane transporter activity Source: EcoCyc
  2. antiporter activity Source: EcoliWiki
  3. choline transmembrane transporter activity Source: EcoCyc
  4. drug:proton antiporter activity Source: EcoCyc
  5. transmembrane transporter activity Source: CACAO

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: EcoliWiki
  2. choline transport Source: EcoCyc
  3. drug export Source: GOC
  4. glycine betaine transport Source: EcoCyc
  5. response to drug Source: EcoliWiki
  6. response to osmotic stress Source: EcoCyc
  7. transmembrane transport Source: GOC
  8. transport Source: EcoliWiki
  9. 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.
RETL1328306-WGS:GSTH-3313-MONOMER.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10629. emrE.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33Cytoplasmic2 Publications
Transmembranei4 – 2118Helical; Name=1Add
BLAST
Topological domaini22 – 3312Periplasmic2 PublicationsAdd
BLAST
Transmembranei34 – 5219Helical; Name=2Add
BLAST
Topological domaini53 – 575Cytoplasmic2 Publications
Transmembranei58 – 8124Helical; Name=3Add
BLAST
Topological domaini82 – 843Periplasmic2 Publications
Transmembranei85 – 10521Helical; Name=4Add
BLAST
Topological domaini106 – 1105Cytoplasmic2 Publications

GO - Cellular componenti

  1. integral component of membrane Source: EcoliWiki
  2. integral component of plasma membrane Source: EcoCyc
  3. membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4 – 41Y → 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 Publication
Mutagenesisi4 – 41Y → F or W: No effect on resistance to toxicants. 1 Publication
Mutagenesisi6 – 61Y → C, F or L: No effect on resistance to toxicants. 1 Publication
Mutagenesisi7 – 71L → C: No substrate binding. Resistance to toxicants is abolished. 1 Publication
Mutagenesisi10 – 101A → C: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication
Mutagenesisi11 – 111I → C: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication
Mutagenesisi14 – 141E → C: No substrate binding. No transport activity. Resistance to toxicants is abolished. 2 Publications
Mutagenesisi14 – 141E → 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 Publications
Mutagenesisi17 – 171G → C: No substrate binding. Resistance to toxicants is abolished. 1 Publication
Mutagenesisi18 – 181T → C: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication
Mutagenesisi40 – 401Y → C, F, L, M, S, T or V: Modifies substrate specificity. 1 Publication
Mutagenesisi53 – 531Y → C: No effect on resistance to toxicants. 1 Publication
Mutagenesisi60 – 601Y → C or F: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication
Mutagenesisi63 – 631W → C or Y: No transport activity. Resistance to toxicants is abolished. 1 Publication
Mutagenesisi63 – 631W → F: Still binds substrate, with two-fold reduction in substrate affinity. Resistance to toxicants is abolished. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 110110Multidrug transporter EmrEPRO_0000108074Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP23895.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-9505N.
STRINGi511145.b0543.

Structurei

Secondary structure

1
110
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2016
Helixi35 – 5117
Helixi59 – 7921
Helixi88 – 10316

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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.

Miscellaneous databases

EvolutionaryTraceiP23895.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2076.
HOGENOMiHOG000268006.
KOiK03297.
OMAiAVFVYQQ.
OrthoDBiEOG69WFSW.
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

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_488830.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73644; AAC73644; b0543.
BAE76318; BAE76318; BAE76318.
GeneIDi12930372.
948442.
KEGGiecj:Y75_p0528.
eco:b0543.
PATRICi32116248. VBIEscCol129921_0564.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi JN0329.
RefSeqi NP_415075.1. NC_000913.3.
YP_488830.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I68 electron microscopy - A/B 1-110 [» ]
3B5D X-ray 3.80 A/B 1-110 [» ]
3B61 X-ray 4.50 A/B/C/D/E/F/G/H 1-110 [» ]
3B62 X-ray 4.40 A/B/C/D 1-110 [» ]
ProteinModelPortali P23895.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9505N.
STRINGi 511145.b0543.

Protein family/group databases

TCDBi 2.A.7.1.3. the drug/metabolite transporter (dmt) superfamily.

Protocols and materials databases

DNASUi 948442.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73644 ; AAC73644 ; b0543 .
BAE76318 ; BAE76318 ; BAE76318 .
GeneIDi 12930372.
948442.
KEGGi ecj:Y75_p0528.
eco:b0543.
PATRICi 32116248. VBIEscCol129921_0564.

Organism-specific databases

EchoBASEi EB0623.
EcoGenei EG10629. emrE.

Phylogenomic databases

eggNOGi COG2076.
HOGENOMi HOG000268006.
KOi K03297.
OMAi AVFVYQQ.
OrthoDBi EOG69WFSW.
PhylomeDBi P23895.

Enzyme and pathway databases

BioCyci EcoCyc:EMRE-MONOMER.
ECOL316407:JW0531-MONOMER.
MetaCyc:EMRE-MONOMER.
RETL1328306-WGS:GSTH-3313-MONOMER.

Miscellaneous databases

EvolutionaryTracei P23895.
PROi P23895.

Gene expression databases

Genevestigatori P23895.

Family and domain databases

InterProi IPR000390. Small_multidrug_res.
[Graphical view ]
Pfami PF00893. Multi_Drug_Res. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the ethidium efflux gene from Escherichia coli."
    Purewal A.S.
    FEMS Microbiol. Lett. 66:229-231(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning and characterization of the mvrC gene of Escherichia coli K-12 which confers resistance against methyl viologen toxicity."
    Morimyo M., Hongo E., Hama-Inaba H., Machida I.
    Nucleic Acids Res. 20:3159-3165(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "EmrE, an Escherichia coli 12-kDa multidrug transporter, exchanges toxic cations and H+ and is soluble in organic solvents."
    Yerushalmi H., Lebendiker M., Schuldiner S.
    J. Biol. Chem. 270:6856-6863(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, KINETIC PARAMETERS.
    Strain: K12 / JM109 / ATCC 53323.
  7. "EmrE, the smallest ion-coupled transporter, provides a unique paradigm for structure-function studies."
    Schuldiner S., Lebendiker M., Yerushalmi H.
    J. Exp. Biol. 200:335-341(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli."
    Yerushalmi H., Schuldiner S.
    J. Biol. Chem. 275:5264-5269(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PH DEPENDENCE, MUTAGENESIS OF GLU-14.
    Strain: K12 / JM109 / ATCC 53323.
  9. "Functional analysis of novel multidrug transporters from human pathogens."
    Ninio S., Rotem D., Schuldiner S.
    J. Biol. Chem. 276:48250-48256(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Small is mighty: EmrE, a multidrug transporter as an experimental paradigm."
    Schuldiner S., Granot D., Mordoch S.S., Ninio S., Rotem D., Soskin M., Tate C.G., Yerushalmi H.
    News Physiol. Sci. 16:130-134(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  11. "An amino acid cluster around the essential Glu-14 is part of the substrate- and proton-binding domain of EmrE, a multidrug transporter from Escherichia coli."
    Gutman N., Steiner-Mordoch S., Schuldiner S.
    J. Biol. Chem. 278:16082-16087(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-7; ALA-10; ILE-11; GLU-14; GLY-17 AND THR-18.
  12. "The membrane topology of EmrE - a small multidrug transporter from Escherichia coli."
    Ninio S., Elbaz Y., Schuldiner S.
    FEBS Lett. 562:193-196(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  13. "New insights into the structure and oligomeric state of the bacterial multidrug transporter EmrE: an unusual asymmetric homo-dimer."
    Ubarretxena-Belandia I., Tate C.G.
    FEBS Lett. 564:234-238(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  14. "EmrE, a multidrug transporter from Escherichia coli, transports monovalent and divalent substrates with the same stoichiometry."
    Rotem D., Schuldiner S.
    J. Biol. Chem. 279:48787-48793(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state."
    Elbaz Y., Steiner-Mordoch S., Danieli T., Schuldiner S.
    Proc. Natl. Acad. Sci. U.S.A. 101:1519-1524(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  16. "Substrate-induced tryptophan fluorescence changes in EmrE, the smallest ion-coupled multidrug transporter."
    Elbaz Y., Tayer N., Steinfels E., Steiner-Mordoch S., Schuldiner S.
    Biochemistry 44:7369-7377(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TRP-63, SUBUNIT.
  17. "Exploring the binding domain of EmrE, the smallest multidrug transporter."
    Sharoni M., Steiner-Mordoch S., Schuldiner S.
    J. Biol. Chem. 280:32849-32855(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE-BINDING CAVITY.
  18. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  19. "Identification of tyrosine residues critical for the function of an ion-coupled multidrug transporter."
    Rotem D., Steiner-Mordoch S., Schuldiner S.
    J. Biol. Chem. 281:18715-18722(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-4; TYR-6; TYR-40; TYR-53 AND TYR-60.
  20. "On parallel and antiparallel topology of a homodimeric multidrug transporter."
    Soskine M., Mark S., Tayer N., Mizrachi R., Schuldiner S.
    J. Biol. Chem. 281:36205-36212(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  21. "NMR investigation of the multidrug transporter EmrE, an integral membrane protein."
    Schwaiger M., Lebendiker M., Yerushalmi H., Coles M., Groeger A., Schwarz C., Schuldiner S., Kessler H.
    Eur. J. Biochem. 254:610-619(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  22. "Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer."
    Ubarretxena-Belandia I., Baldwin J.M., Schuldiner S., Tate C.G.
    EMBO J. 22:6175-6181(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.5 ANGSTROMS) IN COMPLEX WITH THE DRUG TPP(+).
  23. "Structure of the multidrug resistance efflux transporter EmrE from Escherichia coli."
    Ma C., Chang G.
    Proc. Natl. Acad. Sci. U.S.A. 101:2852-2857(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS).
  24. "X-ray structure of the EmrE multidrug transporter in complex with a substrate."
    Pornillos O., Chen Y.-J., Chen A.P., Chang G.
    Science 310:1950-1953(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) IN COMPLEX WITH THE DRUG TPP(+), SUBUNIT.
  25. Cited for: RETRACTION.
  26. "Quasi-symmetry in the cryo-EM structure of EmrE provides the key to modeling its transmembrane domain."
    Fleishman S.J., Harrington S.E., Enosh A., Halperin D., Tate C.G., Ben-Tal N.
    J. Mol. Biol. 364:54-67(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.5 ANGSTROMS), 3D-STRUCTURE MODELING.

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: July 9, 2014
This is version 125 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.

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

External Data

Dasty 3

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