MDTM_ECOLI
ID MDTM_ECOLI Reviewed; 410 AA.
AC P39386; Q2M5X6; Q7X4V2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Multidrug resistance protein MdtM;
GN Name=mdtM; Synonyms=yjiO; OrderedLocusNames=b4337, JW4300;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RA Ramchandani J.H., Bhattacharjee S.K., Mahajan S.K.;
RT "Nucleotide sequence of the YjiO gene of Escherichia coli B.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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.
RX PubMed=11566977; DOI=10.1128/jb.183.20.5803-5812.2001;
RA Nishino K., Yamaguchi A.;
RT "Analysis of a complete library of putative drug transporter genes in
RT Escherichia coli.";
RL J. Bacteriol. 183:5803-5812(2001).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
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).
CC -!- FUNCTION: Confers resistance to acriflavine, chloramphenicol,
CC norfloxacin, ethidium bromide and TPP. {ECO:0000269|PubMed:11566977}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AY283773; AAP43530.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97233.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77293.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78330.1; -; Genomic_DNA.
DR PIR; S56562; S56562.
DR RefSeq; NP_418757.1; NC_000913.3.
DR RefSeq; WP_001137036.1; NZ_LN832404.1.
DR AlphaFoldDB; P39386; -.
DR SMR; P39386; -.
DR BioGRID; 4261450; 183.
DR DIP; DIP-12641N; -.
DR STRING; 511145.b4337; -.
DR TCDB; 2.A.1.2.52; the major facilitator superfamily (mfs).
DR PaxDb; P39386; -.
DR PRIDE; P39386; -.
DR EnsemblBacteria; AAC77293; AAC77293; b4337.
DR EnsemblBacteria; BAE78330; BAE78330; BAE78330.
DR GeneID; 948861; -.
DR KEGG; ecj:JW4300; -.
DR KEGG; eco:b4337; -.
DR PATRIC; fig|1411691.4.peg.2350; -.
DR EchoBASE; EB2464; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_47_2_6; -.
DR InParanoid; P39386; -.
DR OMA; YIPLMSW; -.
DR PhylomeDB; P39386; -.
DR BioCyc; EcoCyc:YJIO-MON; -.
DR BioCyc; MetaCyc:YJIO-MON; -.
DR PRO; PR:P39386; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IDA:EcoCyc.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015721; P:bile acid and bile salt transport; IDA:EcoCyc.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IDA:EcoCyc.
DR GO; GO:0030641; P:regulation of cellular pH; IMP:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:EcoCyc.
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 1: Evidence at protein level;
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_0000084839"
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"
FT VARIANT 128
FT /note="E -> K (in strain: B)"
SQ SEQUENCE 410 AA; 44688 MW; 17C909971AD788B7 CRC64;
MPRFFTRHAA TLFFPMALIL YDFAAYLSTD LIQPGIINVV RDFNADVSLA PAAVSLYLAG
GMALQWLLGP LSDRIGRRPV LITGALIFTL ACAATMFTTS MTQFLIARAI QGTSICFIAT
VGYVTVQEAF GQTKGIKLMA IITSIVLIAP IIGPLSGAAL MHFMHWKVLF AIIAVMGFIS
FVGLLLAMPE TVKRGAVPFS AKSVLRDFRN VFCNRLFLFG AATISLSYIP MMSWVAVSPV
ILIDAGSLTT SQFAWTQVPV FGAVIVANAI VARFVKDPTE PRFIWRAVPI QLVGLSLLIV
GNLLSPHVWL WSVLGTSLYA FGIGLIFPTL FRFTLFSNKL PKGTVSASLN MVILMVMSVS
VEIGRWLWFN GGRLPFHLLA VVAGVIVVFT LAGLLNRVRQ HQAAELVEEQ
