ID   EMRA_ECOLI              Reviewed;         390 AA.
AC   P27303; P77356;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Multidrug export protein EmrA;
GN   Name=emrA; OrderedLocusNames=b2685, JW2660;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=1409590; DOI=10.1073/pnas.89.19.8938;
RA   Lomovskaya O., Lewis K.;
RT   "Emr, an Escherichia coli locus for multidrug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8938-8942(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   REVIEW.
RX   PubMed=8203018; DOI=10.1016/0968-0004(94)90204-6;
RA   Lewis K.;
RT   "Multidrug resistance pumps in bacteria: variations on a theme.";
RL   Trends Biochem. Sci. 19:119-123(1994).
RN   [6]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=12482849; DOI=10.1074/jbc.m209457200;
RA   Borges-Walmsley M.I., Beauchamp J., Kelly S.M., Jumel K., Candlish D.,
RA   Harding S.E., Price N.C., Walmsley A.R.;
RT   "Identification of oligomerization and drug-binding domains of the membrane
RT   fusion protein EmrA.";
RL   J. Biol. Chem. 278:12903-12912(2003).
RN   [7]
RP   INTERACTION WITH EMRB.
RX   PubMed=19171121; DOI=10.1016/j.bbrc.2009.01.081;
RA   Tanabe M., Szakonyi G., Brown K.A., Henderson P.J., Nield J., Byrne B.;
RT   "The multidrug resistance efflux complex, EmrAB from Escherichia coli forms
RT   a dimer in vitro.";
RL   Biochem. Biophys. Res. Commun. 380:338-342(2009).
RN   [8]
RP   INTERACTION WITH TOLC.
RX   PubMed=19805313; DOI=10.1073/pnas.0906601106;
RA   Tikhonova E.B., Dastidar V., Rybenkov V.V., Zgurskaya H.I.;
RT   "Kinetic control of TolC recruitment by multidrug efflux complexes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16416-16421(2009).
CC   -!- FUNCTION: Part of the tripartite efflux system EmrAB-TolC, which
CC       confers resistance to antibiotics such as CCCP, FCCP, 2,4-dinitrophenol
CC       and nalidixic acid. EmrA is a drug-binding protein that provides a
CC       physical link between EmrB and TolC. {ECO:0000269|PubMed:12482849,
CC       ECO:0000269|PubMed:1409590}.
CC   -!- SUBUNIT: Homodimer and homotrimer. Part of the tripartite efflux system
CC       EmrAB-TolC, which is composed of an inner membrane transporter, EmrB, a
CC       periplasmic membrane fusion protein, EmrA, and an outer membrane
CC       component, TolC. The complex forms a large protein conduit and can
CC       translocate molecules across both the inner and outer membranes.
CC       Interacts with EmrB. EmrAB complex forms a dimer in vitro.
CC       {ECO:0000269|PubMed:12482849, ECO:0000269|PubMed:19171121,
CC       ECO:0000269|PubMed:19805313}.
CC   -!- INTERACTION:
CC       P27303; P27303: emrA; NbExp=3; IntAct=EBI-1119547, EBI-1119547;
CC       P27303; P0AEJ0: emrB; NbExp=2; IntAct=EBI-1119547, EBI-21407519;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:12482849,
CC       ECO:0000269|PubMed:1409590}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:12482849, ECO:0000269|PubMed:1409590}; Periplasmic
CC       side {ECO:0000269|PubMed:12482849, ECO:0000269|PubMed:1409590}.
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000305}.
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DR   EMBL; M86657; AAA23724.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75732.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16547.1; -; Genomic_DNA.
DR   PIR; F65048; F65048.
DR   RefSeq; NP_417170.1; NC_000913.3.
DR   RefSeq; WP_001326681.1; NZ_LN832404.1.
DR   AlphaFoldDB; P27303; -.
DR   BioGRID; 4262946; 219.
DR   BioGRID; 851498; 1.
DR   ComplexPortal; CPX-4268; EmrAB-TolC multidrug efflux transport system.
DR   DIP; DIP-9502N; -.
DR   IntAct; P27303; 4.
DR   STRING; 511145.b2685; -.
DR   TCDB; 8.A.1.1.1; the membrane fusion protein (mfp) family.
DR   jPOST; P27303; -.
DR   PaxDb; P27303; -.
DR   PRIDE; P27303; -.
DR   EnsemblBacteria; AAC75732; AAC75732; b2685.
DR   EnsemblBacteria; BAA16547; BAA16547; BAA16547.
DR   GeneID; 947166; -.
DR   KEGG; ecj:JW2660; -.
DR   KEGG; eco:b2685; -.
DR   PATRIC; fig|1411691.4.peg.4054; -.
DR   EchoBASE; EB1329; -.
DR   eggNOG; COG1566; Bacteria.
DR   HOGENOM; CLU_018816_15_0_6; -.
DR   InParanoid; P27303; -.
DR   OMA; VQITPQI; -.
DR   PhylomeDB; P27303; -.
DR   BioCyc; EcoCyc:EG11354-MON; -.
DR   BioCyc; MetaCyc:EG11354-MON; -.
DR   PRO; PR:P27303; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:1990281; C:efflux pump complex; IC:ComplexPortal.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; IMP:EcoliWiki.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0098567; C:periplasmic side of plasma membrane; IC:ComplexPortal.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR   GO; GO:0009636; P:response to toxic substance; IMP:EcoCyc.
DR   GO; GO:0140330; P:xenobiotic detoxification by transmembrane export across the cell outer membrane; IC:ComplexPortal.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:EcoCyc.
DR   InterPro; IPR043602; CusB_dom_1.
DR   InterPro; IPR005694; Efflux_pump_mem.
DR   InterPro; IPR032317; HlyD_D23.
DR   Pfam; PF00529; CusB_dom_1; 1.
DR   Pfam; PF16576; HlyD_D23; 1.
DR   TIGRFAMs; TIGR00998; 8a0101; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane; Coiled coil;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..390
FT                   /note="Multidrug export protein EmrA"
FT                   /id="PRO_0000201869"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..390
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   COILED          120..180
FT                   /evidence="ECO:0000255"
FT   CONFLICT        62
FT                   /note="I -> M (in Ref. 1; AAA23724)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="K -> Q (in Ref. 1; AAA23724)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   390 AA;  42736 MW;  0FB9AE8C20A270F9 CRC64;
     MSANAETQTP QQPVKKSGKR KRLLLLLTLL FIIIAVAIGI YWFLVLRHFE ETDDAYVAGN
     QIQIMSQVSG SVTKVWADNT DFVKEGDVLV TLDPTDARQA FEKAKTALAS SVRQTHQLMI
     NSKQLQANIE VQKIALAKAQ SDYNRRVPLG NANLIGREEL QHARDAVTSA QAQLDVAIQQ
     YNANQAMILG TKLEDQPAVQ QAATEVRNAW LALERTRIIS PMTGYVSRRA VQPGAQISPT
     TPLMAVVPAT NMWVDANFKE TQIANMRIGQ PVTITTDIYG DDVKYTGKVV GLDMGTGSAF
     SLLPAQNATG NWIKVVQRLP VRIELDQKQL EQYPLRIGLS TLVSVNTTNR DGQVLANKVR
     STPVAVSTAR EISLAPVNKL IDDIVKANAG