MDTD_ECOLI
ID MDTD_ECOLI Reviewed; 471 AA.
AC P36554; P76400; Q54A55;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Putative multidrug resistance protein MdtD;
GN Name=mdtD; Synonyms=yegB; OrderedLocusNames=b2077, JW2062;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12;
RX PubMed=12107133; DOI=10.1128/jb.184.15.4161-4167.2002;
RA Nagakubo S., Nishino K., Hirata T., Yamaguchi A.;
RT "The putative response regulator BaeR stimulates multidrug resistance of
RT Escherichia coli via a novel multidrug exporter system, MdtABC.";
RL J. Bacteriol. 184:4161-4167(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 381-471.
RC STRAIN=K12;
RX PubMed=8282725; DOI=10.1093/oxfordjournals.jbchem.a124180;
RA Nagasawa S., Ishige K., Mizuno T.;
RT "Novel members of the two-component signal transduction genes in
RT Escherichia coli.";
RL J. Biochem. 114:350-357(1993).
RN [6]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=12107134; DOI=10.1128/jb.184.15.4168-4176.2002;
RA Baranova N., Nikaido H.;
RT "The baeSR two-component regulatory system activates transcription of the
RT yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and
RT increases its resistance to novobiocin and deoxycholate.";
RL J. Bacteriol. 184:4168-4176(2002).
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 -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Transcriptionally regulated by BaeR.
CC {ECO:0000269|PubMed:12107133, ECO:0000269|PubMed:12107134}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; AB089190; BAC06610.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75138.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15933.1; -; Genomic_DNA.
DR EMBL; D14054; BAA03139.1; -; Genomic_DNA.
DR PIR; D64974; D64974.
DR RefSeq; NP_416581.1; NC_000913.3.
DR RefSeq; WP_000130850.1; NZ_SSZK01000011.1.
DR AlphaFoldDB; P36554; -.
DR SMR; P36554; -.
DR BioGRID; 4260425; 175.
DR DIP; DIP-11876N; -.
DR IntAct; P36554; 2.
DR STRING; 511145.b2077; -.
DR TCDB; 2.A.1.3.26; the major facilitator superfamily (mfs).
DR PaxDb; P36554; -.
DR PRIDE; P36554; -.
DR EnsemblBacteria; AAC75138; AAC75138; b2077.
DR EnsemblBacteria; BAA15933; BAA15933; BAA15933.
DR GeneID; 946601; -.
DR KEGG; ecj:JW2062; -.
DR KEGG; eco:b2077; -.
DR PATRIC; fig|1411691.4.peg.173; -.
DR EchoBASE; EB2057; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_000960_28_0_6; -.
DR InParanoid; P36554; -.
DR OMA; FKIHTFS; -.
DR PhylomeDB; P36554; -.
DR BioCyc; EcoCyc:B2077-MON; -.
DR PRO; PR:P36554; -.
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:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR HAMAP; MF_01577; MFS_MdtD; 1.
DR InterPro; IPR004638; EmrB-like.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR023721; Multi-R_MdtD.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00711; efflux_EmrB; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..471
FT /note="Putative multidrug resistance protein MdtD"
FT /id="PRO_0000173406"
FT TOPO_DOM 1..11
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..76
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..137
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..196
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..262
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..341
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..430
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 471 AA; 50901 MW; FCAF02AD330B5F42 CRC64;
MTDLPDSTRW QLWIVAFGFF MQSLDTTIVN TALPSMAQSL GESPLHMHMV IVSYVLTVAV
MLPASGWLAD KVGVRNIFFT AIVLFTLGSL FCALSGTLNE LLLARALQGV GGAMMVPVGR
LTVMKIVPRE QYMAAMTFVT LPGQVGPLLG PALGGLLVEY ASWHWIFLIN IPVGIIGAIA
TLLLMPNYTM QTRRFDLSGF LLLAVGMAVL TLALDGSKGT GLSPLTIAGL VAVGVVALVL
YLLHARNNNR ALFSLKLFRT RTFSLGLAGS FAGRIGSGML PFMTPVFLQI GLGFSPFHAG
LMMIPMVLGS MGMKRIVVQV VNRFGYRRVL VATTLGLSLV TLLFMTTALL GWYYVLPFVL
FLQGMVNSTR FSSMNTLTLK DLPDNLASSG NSLLSMIMQL SMSIGVTIAG LLLGLFGSQH
VSVDSGTTQT VFMYTWLSMA LIIALPAFIF ARVPNDTHQN VAISRRKRSA Q