MDTH_ECOLI
ID MDTH_ECOLI Reviewed; 402 AA.
AC P69367; P75929; P77042; Q9R7P2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Multidrug resistance protein MdtH;
GN Name=mdtH; Synonyms=yceL; OrderedLocusNames=b1065, JW1052;
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;
RX PubMed=9111025; DOI=10.1074/jbc.272.17.11236;
RA Vlamis-Gardikas A., Aaslund F., Spyrou G., Bergman T., Holmgren A.;
RT "Cloning, overexpression, and characterization of glutaredoxin 2, an
RT atypical glutaredoxin from Escherichia coli.";
RL J. Biol. Chem. 272:11236-11243(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(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 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 INDUCTION.
RC STRAIN=K12;
RX PubMed=15686558; DOI=10.1111/j.1365-2958.2004.04449.x;
RA Hirakawa H., Inazumi Y., Masaki T., Hirata T., Yamaguchi A.;
RT "Indole induces the expression of multidrug exporter genes in Escherichia
RT coli.";
RL Mol. Microbiol. 55:1113-1126(2005).
RN [7]
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 norfloxacin and enoxacin.
CC {ECO:0000269|PubMed:11566977}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Induced at least fivefold by indole in a dose-dependent
CC manner. {ECO:0000269|PubMed:15686558}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC MdtH (TC 2.A.1.2.21) subfamily. {ECO:0000305}.
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DR EMBL; X92076; CAA63057.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74149.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35873.2; -; Genomic_DNA.
DR PIR; F64849; F64849.
DR RefSeq; NP_415583.4; NC_000913.3.
DR RefSeq; WP_000092206.1; NZ_SSZK01000053.1.
DR AlphaFoldDB; P69367; -.
DR SMR; P69367; -.
DR BioGRID; 4260075; 314.
DR IntAct; P69367; 1.
DR STRING; 511145.b1065; -.
DR TCDB; 2.A.1.2.21; the major facilitator superfamily (mfs).
DR PaxDb; P69367; -.
DR PRIDE; P69367; -.
DR EnsemblBacteria; AAC74149; AAC74149; b1065.
DR EnsemblBacteria; BAA35873; BAA35873; BAA35873.
DR GeneID; 946920; -.
DR KEGG; ecj:JW1052; -.
DR KEGG; eco:b1065; -.
DR PATRIC; fig|1411691.4.peg.1203; -.
DR EchoBASE; EB3637; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_001265_60_2_6; -.
DR InParanoid; P69367; -.
DR OMA; TVCVWTL; -.
DR PhylomeDB; P69367; -.
DR BioCyc; EcoCyc:B1065-MON; -.
DR PRO; PR:P69367; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR Gene3D; 1.20.1250.20; -; 1.
DR HAMAP; MF_01529; MFS_MdtH; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR022855; Multidrug-R_MdtH.
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..402
FT /note="Multidrug resistance protein MdtH"
FT /id="PRO_0000173342"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..98
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..164
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..243
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..299
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..367
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 322..323
FT /note="SA -> RS (in Ref. 1; CAA63057)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 44363 MW; 7220F064CD012BB4 CRC64;
MSRVSQARNL GKYFLLIDNM LVVLGFFVVF PLISIRFVDQ MGWAAVMVGI ALGLRQFIQQ
GLGIFGGAIA DRFGAKPMIV TGMLMRAAGF ATMGIAHEPW LLWFSCLLSG LGGTLFDPPR
SALVVKLIRP QQRGRFFSLL MMQDSAGAVI GALLGSWLLQ YDFRLVCATG AVLFVLCAAF
NAWLLPAWKL STVRTPVREG MTRVMRDKRF VTYVLTLAGY YMLAVQVMLM LPIMVNDVAG
APSAVKWMYA IEACLSLTLL YPIARWSEKH FRLEHRLMAG LLIMSLSMMP VGMVSGLQQL
FTLICLFYIG SIIAEPARET LSASLADARA RGSYMGFSRL GLAIGGAIGY IGGGWLFDLG
KSAHQPELPW MMLGIIGIFT FLALGWQFSQ KRAARRLLER DA
