MDTD_SALEP
ID MDTD_SALEP Reviewed; 470 AA.
AC B5R0C2;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Putative multidrug resistance protein MdtD {ECO:0000255|HAMAP-Rule:MF_01577};
GN Name=mdtD {ECO:0000255|HAMAP-Rule:MF_01577}; OrderedLocusNames=SEN2125;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01577}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01577}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000255|HAMAP-Rule:MF_01577}.
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DR EMBL; AM933172; CAR33708.1; -; Genomic_DNA.
DR RefSeq; WP_000137818.1; NC_011294.1.
DR AlphaFoldDB; B5R0C2; -.
DR SMR; B5R0C2; -.
DR KEGG; set:SEN2125; -.
DR HOGENOM; CLU_000960_28_0_6; -.
DR OMA; FKIHTFS; -.
DR Proteomes; UP000000613; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1250.20; -; 1.
DR HAMAP; MF_01577; MFS_MdtD; 1.
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 PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..470
FT /note="Putative multidrug resistance protein MdtD"
FT /id="PRO_0000365285"
FT TOPO_DOM 1..11
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 33..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 70..76
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 98..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 102..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 125..137
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 159..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 186..196
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 218..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 246..262
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 284..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 307..341
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 363..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 417..430
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
FT TOPO_DOM 452..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
SQ SEQUENCE 470 AA; 50780 MW; 93770B509DBCA2FA CRC64;
MTELPDNTRW QLWIVAFGFF MQSLDTTIVN TALPSMAKSL GESPLHMHMV VVSYVLTVAV
MLPASGWLAD KIGVRNIFFA AIVLFTLGSL FCALSGTLNQ LVLARVLQGV GGAMMVPVGR
LTVMKIVPRA QYMAAMTFVT LPGQIGPLLG PALGGVLVEY ASWHWIFLIN IPVGIVGAMA
TFMLMPNYTI ETRRFDLPGF LLLAIGMAVL TLALDGSKSM GISPWTLAGL AAGGAAAILL
YLFHAKKNSG ALFSLRLFRT PTFSLGLLGS FAGRIGSGML PFMTPVFLQI GLGFSPFHAG
LMMIPMVLGS MGMKRIVVQI VNRFGYRRVL VATTLGLALV SLLFMSVALL GWYYLLPLVL
LLQGMVNSAR FSSMNTLTLK DLPDTLASSG NSLLSMIMQL SMSIGVTIAG MLLGMFGQQH
IGIDSSATHH VFMYTWLCMA VIIALPAIIF ARVPNDTQQN MVISRRKRSL
