MDTK_ECOLI
ID MDTK_ECOLI Reviewed; 457 AA.
AC P37340; P77276; P77765;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Multidrug resistance protein MdtK;
DE AltName: Full=Multidrug-efflux transporter;
GN Name=mdtK;
GN Synonyms=norE {ECO:0000303|PubMed:12615854},
GN norM {ECO:0000303|PubMed:9661020}, ydhE; OrderedLocusNames=b1663, JW1655;
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=K12 / MG1655 / ATCC 47076;
RX PubMed=9023191; DOI=10.1128/jb.179.4.1105-1111.1997;
RA Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R.,
RA Holden D.W.;
RT "Analysis of the boundaries of Salmonella pathogenicity island 2 and the
RT corresponding chromosomal region of Escherichia coli K-12.";
RL J. Bacteriol. 179:1105-1111(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
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 SEQUENCE REVISION TO 32.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-230.
RC STRAIN=K12 / RR28;
RA Eberhardt S.M.R., Richter G., Gimbel W., Werner T., Bacher A.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION IN DRUG EXPORT, AND SUBSTRATE SPECIFICITY.
RC STRAIN=K12 / KAM3;
RX PubMed=9661020; DOI=10.1128/aac.42.7.1778;
RA Morita Y., Kodama K., Shiota S., Mine T., Kataoka A., Mizushima T.,
RA Tsuchiya T.;
RT "NorM, a putative multidrug efflux protein, of Vibrio parahaemolyticus and
RT its homolog in Escherichia coli.";
RL Antimicrob. Agents Chemother. 42:1778-1782(1998).
RN [8]
RP IDENTIFICATION OF THE MATE FAMILY.
RX PubMed=9987140; DOI=10.1046/j.1365-2958.1999.01162.x;
RA Brown M.H., Paulsen I.T., Skurray R.A.;
RT "The multidrug efflux protein NorM is a prototype of a new family of
RT transporters.";
RL Mol. Microbiol. 31:394-395(1999).
RN [9]
RP FUNCTION IN DRUG EXPORT, AND SUBSTRATE SPECIFICITY.
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 [10]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12615854; DOI=10.1093/jac/dkg126;
RA Yang S., Clayton S.R., Zechiedrich E.L.;
RT "Relative contributions of the AcrAB, MdfA and NorE efflux pumps to
RT quinolone resistance in Escherichia coli.";
RL J. Antimicrob. Chemother. 51:545-556(2003).
RN [11]
RP SUBCELLULAR LOCATION, AND 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).
RN [12]
RP FUNCTION.
RC STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX PubMed=20067529; DOI=10.1111/j.1574-6968.2009.01879.x;
RA Hayashi M., Tabata K., Yagasaki M., Yonetani Y.;
RT "Effect of multidrug-efflux transporter genes on dipeptide resistance and
RT overproduction in Escherichia coli.";
RL FEMS Microbiol. Lett. 304:12-19(2010).
CC -!- FUNCTION: Multidrug efflux pump that probably functions as a Na(+)/drug
CC antiporter. Confers resistance to many drugs such as fluoroquinolones
CC (norfloxacin, ciprofloxacin, enoxacin) and tetraphenylphosphonium ion
CC (TPP) (PubMed:9661020, PubMed:11566977). Also to deoxycholate,
CC doxorubicin, trimethoprim, chloramphenicol, fosfomycin, ethidium
CC bromide and benzalkonium (PubMed:11566977). Also able to export
CC peptides; when overexpressed, allows cells deleted for multiple
CC peptidases (pepA, pepB, pepD and pepN) to grow in the presence of
CC dipeptides Ala-Gln or Gly-Tyr which otherwise inhibit growth
CC (PubMed:20067529). Cells overexpressing this protein have decreased
CC intracellular levels of Ala-Gln dipeptide, and in a system that
CC produces the Ala-Gln dipeptide overproduction of this protein increases
CC export of the dipeptide (PubMed:20067529).
CC {ECO:0000269|PubMed:11566977, ECO:0000269|PubMed:12615854,
CC ECO:0000269|PubMed:20067529, ECO:0000269|PubMed:9661020}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. MdtK subfamily. {ECO:0000305}.
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DR EMBL; U68703; AAB47941.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48136.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15430.1; -; Genomic_DNA.
DR EMBL; X69109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A64924; A64924.
DR RefSeq; WP_001174940.1; NZ_SSZK01000001.1.
DR RefSeq; YP_025307.1; NC_000913.3.
DR AlphaFoldDB; P37340; -.
DR SMR; P37340; -.
DR BioGRID; 4260264; 205.
DR STRING; 511145.b1663; -.
DR BindingDB; P37340; -.
DR ChEMBL; CHEMBL1681613; -.
DR DrugCentral; P37340; -.
DR TCDB; 2.A.66.1.3; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR jPOST; P37340; -.
DR PaxDb; P37340; -.
DR PRIDE; P37340; -.
DR EnsemblBacteria; AAT48136; AAT48136; b1663.
DR EnsemblBacteria; BAA15430; BAA15430; BAA15430.
DR GeneID; 945883; -.
DR KEGG; ecj:JW1655; -.
DR KEGG; eco:b1663; -.
DR PATRIC; fig|1411691.4.peg.594; -.
DR EchoBASE; EB2300; -.
DR eggNOG; COG0534; Bacteria.
DR HOGENOM; CLU_012893_6_0_6; -.
DR InParanoid; P37340; -.
DR OMA; EFWILLK; -.
DR PhylomeDB; P37340; -.
DR BioCyc; EcoCyc:YDHE-MON; -.
DR BioCyc; MetaCyc:YDHE-MON; -.
DR PRO; PR:P37340; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015298; F:solute:cation antiporter activity; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:EcoliWiki.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:EcoCyc.
DR GO; GO:0035442; P:dipeptide transmembrane transport; IMP:EcoCyc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:EcoCyc.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0042908; P:xenobiotic transport; IMP:EcoCyc.
DR HAMAP; MF_00400; MdtK; 1.
DR InterPro; IPR002528; MATE_fam.
DR InterPro; IPR022913; Multidrug-R_MdtK.
DR Pfam; PF01554; MatE; 2.
DR PIRSF; PIRSF006603; DinF; 1.
DR TIGRFAMs; TIGR00797; matE; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Antiport; Cell inner membrane; Cell membrane;
KW Ion transport; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..457
FT /note="Multidrug resistance protein MdtK"
FT /id="PRO_0000164181"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..52
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..126
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..188
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..275
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..349
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..417
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT CONFLICT 32
FT /note="D -> S (in Ref. 1; AAB47941)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="V -> A (in Ref. 6; X69109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 49447 MW; 33A60FC42ED6CFD7 CRC64;
MQKYISEARL LLALAIPVIL AQIAQTAMGF VDTVMAGGYS ATDMAAVAIG TSIWLPAILF
GHGLLLALTP VIAQLNGSGR RERIAHQVRQ GFWLAGFVSV LIMLVLWNAG YIIRSMENID
PALADKAVGY LRALLWGAPG YLFFQVARNQ CEGLAKTKPG MVMGFIGLLV NIPVNYIFIY
GHFGMPELGG VGCGVATAAV YWVMFLAMVS YIKRARSMRD IRNEKGTAKP DPAVMKRLIQ
LGLPIALALF FEVTLFAVVA LLVSPLGIVD VAGHQIALNF SSLMFVLPMS LAAAVTIRVG
YRLGQGSTLD AQTAARTGLM VGVCMATLTA IFTVSLREQI ALLYNDNPEV VTLAAHLMLL
AAVYQISDSI QVIGSGILRG YKDTRSIFYI TFTAYWVLGL PSGYILALTD LVVEPMGPAG
FWIGFIIGLT SAAIMMMLRM RFLQRLPSAI ILQRASR
