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P23895

- EMRE_ECOLI

UniProt

P23895 - EMRE_ECOLI

Protein

Multidrug transporter EmrE

Gene

emrE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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 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)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

    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

    GO - Cellular componenti

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23895.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 33Cytoplasmic
    Topological domaini22 – 3312PeriplasmicAdd
    BLAST
    Topological domaini53 – 575Cytoplasmic
    Topological domaini82 – 843Periplasmic
    Topological domaini106 – 1105Cytoplasmic

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4 – 2118Helical; Name=1Add
    BLAST
    Transmembranei34 – 5219Helical; Name=2Add
    BLAST
    Transmembranei58 – 8124Helical; Name=3Add
    BLAST
    Transmembranei85 – 10521Helical; Name=4Add
    BLAST

    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

    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: October 1, 2014
    This is version 126 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

    External Data

    Dasty 3