MDTM_ECO57
ID MDTM_ECO57 Reviewed; 410 AA.
AC Q8XB84; Q7A8L0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Multidrug resistance protein MdtM;
GN Name=mdtM; OrderedLocusNames=Z5939, ECs5300;
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: Confers resistance to acriflavine, chloramphenicol,
CC norfloxacin, ethidium bromide and TPP. {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.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG59522.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38723.1; -; Genomic_DNA.
DR PIR; D91291; D91291.
DR PIR; F86132; F86132.
DR RefSeq; NP_313327.1; NC_002695.1.
DR RefSeq; WP_001136983.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XB84; -.
DR SMR; Q8XB84; -.
DR STRING; 155864.EDL933_5680; -.
DR EnsemblBacteria; AAG59522; AAG59522; Z5939.
DR EnsemblBacteria; BAB38723; BAB38723; ECs_5300.
DR GeneID; 913623; -.
DR KEGG; ece:Z5939; -.
DR KEGG; ecs:ECs_5300; -.
DR PATRIC; fig|386585.9.peg.5542; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_47_2_6; -.
DR OMA; YIPLMSW; -.
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 InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 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..410
FT /note="Multidrug resistance protein MdtM"
FT /id="PRO_0000084840"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..48
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..103
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..167
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..251
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..307
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..373
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 410 AA; 44523 MW; 523F8169CC4DE1AF CRC64;
MPRFFARHAA TLFFPMALIL YDFAAYLSTD LIQPGIINVV RDFNADVSLA PAAVSLYLAG
GMALQWLLGP LSDRIGRKPV LITGALIFTL ACAATMFTTS MTQFLIARAI QGTSICFIAT
VGYVTVQEAF GQTKGIKLMA IITSIVLIAP IIGPLSGAAL MHFVHWKVLF AIIAVMGFIS
FVGLLLAMPE TVKRGAVPFS AKSVLRDFRN VFCNRLFLFG AATISLSYIP MMSWVAVSPV
ILIDAGGLTT SQFAWTQVPV FGAVIVANAI VARFVKDPTE PRFIWRAVPI QLVGLALLII
GNLLSPHVWL WSVLGTSLYA FGIGLIFPTL FRFTLFSNNL PKGTVSASLN MVILMVMSVS
VEIGRWLWFN GGRLPFHLLA VVAGVIVVFT LAGLLNRVRQ HQAAELAEEQ
