EMRB_ECOLI
ID EMRB_ECOLI Reviewed; 512 AA.
AC P0AEJ0; P27304; P77725;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Multidrug export protein EmrB;
GN Name=emrB; OrderedLocusNames=b2686, JW2661;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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 FUNCTION, AND SUBUNIT.
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 [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP INTERACTION WITH EMRA.
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).
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. {ECO:0000269|PubMed:12482849,
CC ECO:0000269|PubMed:1409590}.
CC -!- SUBUNIT: Part of the tripartite efflux system EmrAB-TolC, which is
CC composed of an inner membrane transporter, EmrB, a periplasmic membrane
CC fusion protein, EmrA, and an outer membrane component, TolC. The
CC complex forms a large protein conduit and can translocate molecules
CC across both the inner and outer membranes. Interacts with EmrA. EmrAB
CC complex forms a dimer in vitro. {ECO:0000269|PubMed:12482849,
CC ECO:0000269|PubMed:19171121}.
CC -!- INTERACTION:
CC P0AEJ0; P27303: emrA; NbExp=2; IntAct=EBI-21407519, EBI-1119547;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. EmrB family.
CC {ECO:0000305}.
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DR EMBL; M86657; AAA23725.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75733.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16548.1; -; Genomic_DNA.
DR PIR; G65048; G65048.
DR RefSeq; NP_417171.1; NC_000913.3.
DR RefSeq; WP_001295176.1; NZ_STEB01000042.1.
DR AlphaFoldDB; P0AEJ0; -.
DR SMR; P0AEJ0; -.
DR BioGRID; 4263179; 251.
DR ComplexPortal; CPX-4268; EmrAB-TolC multidrug efflux transport system.
DR IntAct; P0AEJ0; 1.
DR STRING; 511145.b2686; -.
DR TCDB; 2.A.1.3.2; the major facilitator superfamily (mfs).
DR PaxDb; P0AEJ0; -.
DR PRIDE; P0AEJ0; -.
DR EnsemblBacteria; AAC75733; AAC75733; b2686.
DR EnsemblBacteria; BAA16548; BAA16548; BAA16548.
DR GeneID; 66673445; -.
DR GeneID; 947167; -.
DR KEGG; ecj:JW2661; -.
DR KEGG; eco:b2686; -.
DR PATRIC; fig|1411691.4.peg.4053; -.
DR EchoBASE; EB1409; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_000960_28_0_6; -.
DR InParanoid; P0AEJ0; -.
DR OMA; GNICYGA; -.
DR PhylomeDB; P0AEJ0; -.
DR BioCyc; EcoCyc:EMRB-MON; -.
DR BioCyc; MetaCyc:EMRB-MON; -.
DR PRO; PR:P0AEJ0; -.
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; ISM:EcoCyc.
DR GO; GO:0098567; C:periplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IMP:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR004638; EmrB-like.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00711; efflux_EmrB; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..512
FT /note="Multidrug export protein EmrB"
FT /id="PRO_0000173322"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..51
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..164
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 325
FT /note="G -> A (in Ref. 1; AAA23725)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="P -> A (in Ref. 1; AAA23725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 55624 MW; 070334E68B303EFF CRC64;
MQQQKPLEGA QLVIMTIALS LATFMQVLDS TIANVAIPTI AGNLGSSLSQ GTWVITSFGV
ANAISIPLTG WLAKRVGEVK LFLWSTIAFA IASWACGVSS SLNMLIFFRV IQGIVAGPLI
PLSQSLLLNN YPPAKRSIAL ALWSMTVIVA PICGPILGGY ISDNYHWGWI FFINVPIGVA
VVLMTLQTLR GRETRTERRR IDAVGLALLV IGIGSLQIML DRGKELDWFS SQEIIILTVV
AVVAICFLIV WELTDDNPIV DLSLFKSRNF TIGCLCISLA YMLYFGAIVL LPQLLQEVYG
YTATWAGLAS APVGIIPVIL SPIIGRFAHK LDMRRLVTFS FIMYAVCFYW RAYTFEPGMD
FGASAWPQFI QGFAVACFFM PLTTITLSGL PPERLAAASS LSNFTRTLAG SIGTSITTTM
WTNRESMHHA QLTESVNPFN PNAQAMYSQL EGLGMTQQQA SGWIAQQITN QGLIISANEI
FWMSAGIFLV LLGLVWFAKP PFGAGGGGGG AH
