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Multidrug transporter EmrE (Efflux-multidrug resistance protein EmrE) (Ethidium resistance protein) (Methyl viologen resistance protein C)

 EMRE_ECOLI              Reviewed;         110 AA.
P23895; Q2MBN8;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 1.
12-SEP-2018, entry version 148.
RecName: Full=Multidrug transporter EmrE;
AltName: Full=Efflux-multidrug resistance protein EmrE;
AltName: Full=Ethidium resistance protein;
AltName: Full=Methyl viologen resistance protein C;
Name=emrE; Synonyms=eb, mvrC; OrderedLocusNames=b0543, JW0531;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1936950; DOI=10.1016/0378-1097(91)90338-B;
Purewal A.S.;
"Nucleotide sequence of the ethidium efflux gene from Escherichia
coli.";
FEMS Microbiol. Lett. 66:229-231(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1320256; DOI=10.1093/nar/20.12.3159;
Morimyo M., Hongo E., Hama-Inaba H., Machida I.;
"Cloning and characterization of the mvrC gene of Escherichia coli K-
12 which confers resistance against methyl viologen toxicity.";
Nucleic Acids Res. 20:3159-3165(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
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.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
FUNCTION, AND KINETIC PARAMETERS.
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=7896833; DOI=10.1074/jbc.270.12.6856;
Yerushalmi H., Lebendiker M., Schuldiner S.;
"EmrE, an Escherichia coli 12-kDa multidrug transporter, exchanges
toxic cations and H+ and is soluble in organic solvents.";
J. Biol. Chem. 270:6856-6863(1995).
[7]
CHARACTERIZATION.
PubMed=9050242;
Schuldiner S., Lebendiker M., Yerushalmi H.;
"EmrE, the smallest ion-coupled transporter, provides a unique
paradigm for structure-function studies.";
J. Exp. Biol. 200:335-341(1997).
[8]
FUNCTION, PH DEPENDENCE, AND MUTAGENESIS OF GLU-14.
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=10681497; DOI=10.1074/jbc.275.8.5264;
Yerushalmi H., Schuldiner S.;
"An essential glutamyl residue in EmrE, a multidrug antiporter from
Escherichia coli.";
J. Biol. Chem. 275:5264-5269(2000).
[9]
FUNCTION.
PubMed=11574548; DOI=10.1074/jbc.M108231200;
Ninio S., Rotem D., Schuldiner S.;
"Functional analysis of novel multidrug transporters from human
pathogens.";
J. Biol. Chem. 276:48250-48256(2001).
[10]
REVIEW.
PubMed=11443233;
Schuldiner S., Granot D., Mordoch S.S., Ninio S., Rotem D., Soskin M.,
Tate C.G., Yerushalmi H.;
"Small is mighty: EmrE, a multidrug transporter as an experimental
paradigm.";
News Physiol. Sci. 16:130-134(2001).
[11]
MUTAGENESIS OF LEU-7; ALA-10; ILE-11; GLU-14; GLY-17 AND THR-18.
PubMed=12590142; DOI=10.1074/jbc.M213120200;
Gutman N., Steiner-Mordoch S., Schuldiner S.;
"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.";
J. Biol. Chem. 278:16082-16087(2003).
[12]
TOPOLOGY.
PubMed=15044024; DOI=10.1016/S0014-5793(04)00240-6;
Ninio S., Elbaz Y., Schuldiner S.;
"The membrane topology of EmrE - a small multidrug transporter from
Escherichia coli.";
FEBS Lett. 562:193-196(2004).
[13]
SUBUNIT.
PubMed=15111102; DOI=10.1016/S0014-5793(04)00228-5;
Ubarretxena-Belandia I., Tate C.G.;
"New insights into the structure and oligomeric state of the bacterial
multidrug transporter EmrE: an unusual asymmetric homo-dimer.";
FEBS Lett. 564:234-238(2004).
[14]
FUNCTION.
PubMed=15371426; DOI=10.1074/jbc.M408187200;
Rotem D., Schuldiner S.;
"EmrE, a multidrug transporter from Escherichia coli, transports
monovalent and divalent substrates with the same stoichiometry.";
J. Biol. Chem. 279:48787-48793(2004).
[15]
SUBUNIT.
PubMed=14755055; DOI=10.1073/pnas.0306533101;
Elbaz Y., Steiner-Mordoch S., Danieli T., Schuldiner S.;
"In vitro synthesis of fully functional EmrE, a multidrug transporter,
and study of its oligomeric state.";
Proc. Natl. Acad. Sci. U.S.A. 101:1519-1524(2004).
[16]
MUTAGENESIS OF TRP-63, AND SUBUNIT.
PubMed=15882076; DOI=10.1021/bi050356t;
Elbaz Y., Tayer N., Steinfels E., Steiner-Mordoch S., Schuldiner S.;
"Substrate-induced tryptophan fluorescence changes in EmrE, the
smallest ion-coupled multidrug transporter.";
Biochemistry 44:7369-7377(2005).
[17]
SUBSTRATE-BINDING CAVITY.
PubMed=16049002; DOI=10.1074/jbc.M504910200;
Sharoni M., Steiner-Mordoch S., Schuldiner S.;
"Exploring the binding domain of EmrE, the smallest multidrug
transporter.";
J. Biol. Chem. 280:32849-32855(2005).
[18]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[19]
MUTAGENESIS OF TYR-4; TYR-6; TYR-40; TYR-53 AND TYR-60.
PubMed=16672221; DOI=10.1074/jbc.M602088200;
Rotem D., Steiner-Mordoch S., Schuldiner S.;
"Identification of tyrosine residues critical for the function of an
ion-coupled multidrug transporter.";
J. Biol. Chem. 281:18715-18722(2006).
[20]
SUBUNIT.
PubMed=17003034; DOI=10.1074/jbc.M607186200;
Soskine M., Mark S., Tayer N., Mizrachi R., Schuldiner S.;
"On parallel and antiparallel topology of a homodimeric multidrug
transporter.";
J. Biol. Chem. 281:36205-36212(2006).
[21]
STRUCTURE BY NMR.
PubMed=9688273; DOI=10.1046/j.1432-1327.1998.2540610.x;
Schwaiger M., Lebendiker M., Yerushalmi H., Coles M., Groeger A.,
Schwarz C., Schuldiner S., Kessler H.;
"NMR investigation of the multidrug transporter EmrE, an integral
membrane protein.";
Eur. J. Biochem. 254:610-619(1998).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (7.5 ANGSTROMS) IN COMPLEX WITH THE
DRUG TPP(+).
PubMed=14633977; DOI=10.1093/emboj/cdg611;
Ubarretxena-Belandia I., Baldwin J.M., Schuldiner S., Tate C.G.;
"Three-dimensional structure of the bacterial multidrug transporter
EmrE shows it is an asymmetric homodimer.";
EMBO J. 22:6175-6181(2003).
[23]
X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS).
PubMed=14970332; DOI=10.1073/pnas.0400137101;
Ma C., Chang G.;
"Structure of the multidrug resistance efflux transporter EmrE from
Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 101:2852-2857(2004).
[24]
X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) IN COMPLEX WITH THE DRUG TPP(+),
AND SUBUNIT.
PubMed=16373573; DOI=10.1126/science.1119776;
Pornillos O., Chen Y.-J., Chen A.P., Chang G.;
"X-ray structure of the EmrE multidrug transporter in complex with a
substrate.";
Science 310:1950-1953(2005).
[25]
ERRATUM, AND RETRACTION.
PubMed=17185584; DOI=10.1126/science.314.5807.1875b;
Chang G., Roth C.B., Reyes C.L., Pornillos O., Chen Y.J., Chen A.P.;
Science 314:1875-1875(2006).
[26]
STRUCTURE BY ELECTRON MICROSCOPY (7.5 ANGSTROMS), AND 3D-STRUCTURE
MODELING.
PubMed=17005200; DOI=10.1016/j.jmb.2006.08.072;
Fleishman S.J., Harrington S.E., Enosh A., Halperin D., Tate C.G.,
Ben-Tal N.;
"Quasi-symmetry in the cryo-EM structure of EmrE provides the key to
modeling its transmembrane domain.";
J. Mol. Biol. 364:54-67(2006).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10681497,
ECO:0000269|PubMed:11574548, ECO:0000269|PubMed:15371426,
ECO:0000269|PubMed:7896833}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=247 uM for methyl viologen {ECO:0000269|PubMed:7896833};
Vmax=1572 nmol/min/mg enzyme with methyl viologen as substrate
{ECO:0000269|PubMed:7896833};
pH dependence:
Optimum pH is 8-8.5. Transport activity occurs from pH 7.5 to 9.
{ECO:0000269|PubMed:10681497};
-!- SUBUNIT: Homodimer; parallel. May also form dimer of homodimers.
Binds substrate at the dimerization interface.
{ECO:0000269|PubMed:14755055, ECO:0000269|PubMed:15111102,
ECO:0000269|PubMed:15882076, ECO:0000269|PubMed:16373573,
ECO:0000269|PubMed:17003034}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-8789431, EBI-8789431;
-!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
protein.
-!- MISCELLANEOUS: Encoded by the cryptic lambdoid prophage DLP12.
-!- SIMILARITY: Belongs to the small multidrug resistance (SMR)
protein family. {ECO:0000305}.
-!- 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. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z11877; CAA77936.1; -; Genomic_DNA.
EMBL; M62732; AAA24190.1; -; Genomic_DNA.
EMBL; U82598; AAB40740.1; -; Genomic_DNA.
EMBL; U00096; AAC73644.1; -; Genomic_DNA.
EMBL; AP009048; BAE76318.1; -; Genomic_DNA.
PIR; JN0329; JN0329.
RefSeq; NP_415075.1; NC_000913.3.
RefSeq; WP_001070439.1; NZ_LN832404.1.
PDB; 2I68; EM; -; A/B=1-110.
PDB; 3B5D; X-ray; 3.80 A; A/B=1-110.
PDB; 3B61; X-ray; 4.50 A; A/B/C/D/E/F/G/H=1-110.
PDB; 3B62; X-ray; 4.40 A; A/B/C/D=1-110.
PDBsum; 2I68; -.
PDBsum; 3B5D; -.
PDBsum; 3B61; -.
PDBsum; 3B62; -.
ProteinModelPortal; P23895; -.
SMR; P23895; -.
BioGrid; 4259366; 101.
ComplexPortal; CPX-2121; EmrE complex.
DIP; DIP-9505N; -.
STRING; 316385.ECDH10B_0499; -.
TCDB; 2.A.7.1.3; the drug/metabolite transporter (dmt) superfamily.
PaxDb; P23895; -.
PRIDE; P23895; -.
DNASU; 948442; -.
EnsemblBacteria; AAC73644; AAC73644; b0543.
EnsemblBacteria; BAE76318; BAE76318; BAE76318.
GeneID; 948442; -.
KEGG; ecj:JW0531; -.
KEGG; eco:b0543; -.
PATRIC; fig|1411691.4.peg.1735; -.
EchoBASE; EB0623; -.
EcoGene; EG10629; emrE.
eggNOG; ENOG410814C; Bacteria.
eggNOG; COG2076; LUCA.
HOGENOM; HOG000268006; -.
InParanoid; P23895; -.
KO; K03297; -.
OMA; GVVYGTW; -.
PhylomeDB; P23895; -.
BioCyc; EcoCyc:EMRE-MONOMER; -.
BioCyc; MetaCyc:EMRE-MONOMER; -.
SABIO-RK; P23895; -.
EvolutionaryTrace; P23895; -.
PRO; PR:P23895; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
GO; GO:0016020; C:membrane; IDA:EcoliWiki.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0015199; F:amino-acid betaine transmembrane transporter activity; IMP:EcoCyc.
GO; GO:0015297; F:antiporter activity; IDA:EcoliWiki.
GO; GO:0015220; F:choline transmembrane transporter activity; IMP:EcoCyc.
GO; GO:0015307; F:drug:proton antiporter activity; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0022857; F:transmembrane transporter activity; IDA:CACAO.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
GO; GO:0015871; P:choline transport; IMP:EcoCyc.
GO; GO:0031460; P:glycine betaine transport; IMP:EcoCyc.
GO; GO:0042493; P:response to drug; IMP:EcoliWiki.
GO; GO:0006970; P:response to osmotic stress; IMP:EcoCyc.
GO; GO:0006805; P:xenobiotic metabolic process; IMP:EcoliWiki.
InterPro; IPR000390; Small_multidrug_res.
PANTHER; PTHR30561; PTHR30561; 1.
Pfam; PF00893; Multi_Drug_Res; 1.
1: Evidence at protein level;
3D-structure; Antiport; Cell inner membrane; Cell membrane;
Complete proteome; Membrane; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 110 Multidrug transporter EmrE.
/FTId=PRO_0000108074.
TOPO_DOM 1 3 Cytoplasmic.
TRANSMEM 4 21 Helical; Name=1.
TOPO_DOM 22 33 Periplasmic.
TRANSMEM 34 52 Helical; Name=2.
TOPO_DOM 53 57 Cytoplasmic.
TRANSMEM 58 81 Helical; Name=3.
TOPO_DOM 82 84 Periplasmic.
TRANSMEM 85 105 Helical; Name=4.
TOPO_DOM 106 110 Cytoplasmic.
SITE 4 4 Required for proper coupling between the
substrate transport and the proton
gradient.
SITE 14 14 Essential for translocation and for
substrate and proton binding.
SITE 40 40 Involved in substrate binding.
SITE 60 60 Involved in substrate binding.
SITE 63 63 Involved in substrate binding.
MUTAGEN 4 4 Y->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.
{ECO:0000269|PubMed:16672221}.
MUTAGEN 4 4 Y->F,W: No effect on resistance to
toxicants. {ECO:0000269|PubMed:16672221}.
MUTAGEN 6 6 Y->C,F,L: No effect on resistance to
toxicants. {ECO:0000269|PubMed:16672221}.
MUTAGEN 7 7 L->C: No substrate binding. Resistance to
toxicants is abolished.
{ECO:0000269|PubMed:12590142}.
MUTAGEN 10 10 A->C: Still binds substrate, with lower
affinity. Resistance to toxicants is
abolished. {ECO:0000269|PubMed:12590142}.
MUTAGEN 11 11 I->C: Still binds substrate, with lower
affinity. Resistance to toxicants is
abolished. {ECO:0000269|PubMed:12590142}.
MUTAGEN 14 14 E->C: No substrate binding. No transport
activity. Resistance to toxicants is
abolished. {ECO:0000269|PubMed:10681497,
ECO:0000269|PubMed:12590142}.
MUTAGEN 14 14 E->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.
{ECO:0000269|PubMed:10681497,
ECO:0000269|PubMed:12590142}.
MUTAGEN 17 17 G->C: No substrate binding. Resistance to
toxicants is abolished.
{ECO:0000269|PubMed:12590142}.
MUTAGEN 18 18 T->C: Still binds substrate, with lower
affinity. Resistance to toxicants is
abolished. {ECO:0000269|PubMed:12590142}.
MUTAGEN 40 40 Y->C,F,L,M,S,T,V: Modifies substrate
specificity.
{ECO:0000269|PubMed:16672221}.
MUTAGEN 53 53 Y->C: No effect on resistance to
toxicants. {ECO:0000269|PubMed:16672221}.
MUTAGEN 60 60 Y->C,F: Still binds substrate, with lower
affinity. Resistance to toxicants is
abolished. {ECO:0000269|PubMed:16672221}.
MUTAGEN 63 63 W->C,Y: No transport activity. Resistance
to toxicants is abolished.
{ECO:0000269|PubMed:15882076}.
MUTAGEN 63 63 W->F: Still binds substrate, with two-
fold reduction in substrate affinity.
Resistance to toxicants is abolished.
{ECO:0000269|PubMed:15882076}.
HELIX 5 20 {ECO:0000244|PDB:2I68}.
HELIX 35 51 {ECO:0000244|PDB:2I68}.
HELIX 59 79 {ECO:0000244|PDB:2I68}.
HELIX 88 103 {ECO:0000244|PDB:2I68}.
SEQUENCE 110 AA; 11958 MW; 775153FC47D6AE3D CRC64;
MNPYIYLGGA ILAEVIGTTL MKFSEGFTRL WPSVGTIICY CASFWLLAQT LAYIPTGIAY
AIWSGVGIVL ISLLSWGFFG QRLDLPAIIG MMLICAGVLI INLLSRSTPH


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