MDTD_ECO8A
ID MDTD_ECO8A Reviewed; 471 AA.
AC B7M460;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Putative multidrug resistance protein MdtD {ECO:0000255|HAMAP-Rule:MF_01577};
GN Name=mdtD {ECO:0000255|HAMAP-Rule:MF_01577}; OrderedLocusNames=ECIAI1_2153;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAQ98999.1; -; Genomic_DNA.
DR RefSeq; WP_000130898.1; NC_011741.1.
DR AlphaFoldDB; B7M460; -.
DR SMR; B7M460; -.
DR KEGG; ecr:ECIAI1_2153; -.
DR HOGENOM; CLU_000960_28_0_6; -.
DR OMA; FKIHTFS; -.
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; 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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..471
FT /note="Putative multidrug resistance protein MdtD"
FT /id="PRO_1000200777"
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..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01577"
SQ SEQUENCE 471 AA; 50997 MW; EC22C370E89CBC9F CRC64;
MTDLPDSTRW QLWIVAFGFF MQSLDTTIVN TALPSMAQSL GESPLHMHMV IVSYVLTVAV
MLPASGWLAD KVGVRNIFFT AIVLFTLGSL FCALSGTLNE LLLARALQGV GGAMMVPVGR
LTVMKIVPRE QYMAAMTFVT LPGQVGPLLG PALGGLLVEY ASWHWIFLIN IPVGIIGAIA
TLMLMPNYTM QTRRFDLSGF LLLAVGMAVL TLALDGSKGT GLSPLTIDGL VAVGVVALVL
YLLHARNNNR ALFSLKLFRT RTFSLGLAGS FAGRIGSGML PFMTPVFLQI GLGFSPFHAG
LMMIPMVLGS MGMKRIVVQV VNRFGYRRVL VATTLGLSLV TLLFMTTALL GWYYVLPFVL
FLQGMVNSTR FSSMNTLTLK DLPDNLASSG NSLLSMIMQL SMSIGVTIAG LLLGLFGSQH
VSVDSGTTQT VFMYTWLSMA FIIALPAFIF ARVPNDTHQN VAISRRKRSA Q
