EMRB_ECO57
ID EMRB_ECO57 Reviewed; 512 AA.
AC P0AEJ1; P27304; P77725;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Multidrug export protein EmrB;
GN Name=emrB; OrderedLocusNames=Z3987, ECs3548;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Part of the tripartite efflux system EmrAB-TolC, which
CC confers resistance to antibiotics. {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. EmrB family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG57795.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36971.1; -; Genomic_DNA.
DR PIR; D91072; D91072.
DR RefSeq; NP_311575.1; NC_002695.1.
DR RefSeq; WP_001295176.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEJ1; -.
DR SMR; P0AEJ1; -.
DR STRING; 155864.EDL933_3853; -.
DR EnsemblBacteria; AAG57795; AAG57795; Z3987.
DR EnsemblBacteria; BAB36971; BAB36971; ECs_3548.
DR GeneID; 66673445; -.
DR GeneID; 914736; -.
DR KEGG; ece:Z3987; -.
DR KEGG; ecs:ECs_3548; -.
DR PATRIC; fig|386585.9.peg.3704; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_000960_28_0_6; -.
DR OMA; GNICYGA; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 3: Inferred from homology;
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_0000173323"
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"
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
