ID   MDTH_ECO5E              Reviewed;         402 AA.
AC   B5YVT5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Multidrug resistance protein MdtH {ECO:0000255|HAMAP-Rule:MF_01529};
GN   Name=mdtH {ECO:0000255|HAMAP-Rule:MF_01529};
GN   OrderedLocusNames=ECH74115_1444;
OS   Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=444450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC4115 / EHEC;
RX   PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA   Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
CC   -!- FUNCTION: Confers resistance to norfloxacin and enoxacin.
CC       {ECO:0000255|HAMAP-Rule:MF_01529}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01529}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01529}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC       MdtH (TC 2.A.1.2.21) subfamily. {ECO:0000255|HAMAP-Rule:MF_01529}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001164; ACI39213.1; -; Genomic_DNA.
DR   RefSeq; WP_000092209.1; NC_011353.1.
DR   AlphaFoldDB; B5YVT5; -.
DR   SMR; B5YVT5; -.
DR   KEGG; ecf:ECH74115_1444; -.
DR   HOGENOM; CLU_001265_60_2_6; -.
DR   OMA; TVCVWTL; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; 2.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..402
FT                   /note="Multidrug resistance protein MdtH"
FT                   /id="PRO_1000200797"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TOPO_DOM        34..98
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TRANSMEM        99..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TOPO_DOM        117..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TOPO_DOM        160..164
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TOPO_DOM        186..213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TOPO_DOM        235..243
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TOPO_DOM        265..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TOPO_DOM        298..299
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TOPO_DOM        321..339
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TOPO_DOM        361..367
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT   TOPO_DOM        389..402
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
SQ   SEQUENCE   402 AA;  44391 MW;  F0AACB64CD012BAA 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
     KSVHQPELPW MMLGIIGIFT FLALGWQFSQ KRAARRLLER DA