MDTH_YERPS
ID MDTH_YERPS Reviewed; 401 AA.
AC Q66AV8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Multidrug resistance protein MdtH {ECO:0000255|HAMAP-Rule:MF_01529};
GN Name=mdtH {ECO:0000255|HAMAP-Rule:MF_01529}; OrderedLocusNames=YPTB2022;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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}.
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DR EMBL; BX936398; CAH21260.1; -; Genomic_DNA.
DR RefSeq; WP_002211217.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66AV8; -.
DR SMR; Q66AV8; -.
DR EnsemblBacteria; CAH21260; CAH21260; YPTB2022.
DR GeneID; 66841545; -.
DR KEGG; ypo:BZ17_443; -.
DR KEGG; yps:YPTB2022; -.
DR PATRIC; fig|273123.14.peg.473; -.
DR OMA; TVCVWTL; -.
DR Proteomes; UP000001011; Chromosome.
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 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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..401
FT /note="Multidrug resistance protein MdtH"
FT /id="PRO_0000173353"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 99..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01529"
SQ SEQUENCE 401 AA; 44285 MW; 70A8A60C457B219B CRC64;
MALVSQARSL GKYFLLFDNL LVVLGFFVVF PLISIRFVDQ LGWAALVVGL ALGLRQLVQQ
GLGIFGGAIA DRFGAKPMIV TGMLMRAAGF ALMAMADEPW ILWLACALSG LGGTLFDPPR
TALVIKLTRP HERGRFYSLL MMQDSAGAVI GALIGSWLLQ YDFHFVCWTG AAIFVLAAGW
NAWLLPAYRI STVRAPMKEG LMRVLRDRRF VTYVLTLTGY YMLAVQVMLM LPIVVNELAG
SPAAVKWMYA IEAALSLTLL YPLARWSEKR FSLEQRLMAG LLIMTLSLFP IGMITHLQTL
FMFICFFYMG SILAEPARET LGASLADSRA RGSYMGFSRL GLALGGALGY TGGGWMYDTG
KTLDMPELPW FLLGIIGLIT LAGLYWQFNR RRIESAMLSS S