MDTH_SHIFL
ID MDTH_SHIFL Reviewed; 402 AA.
AC Q83LI8; Q7UCX4;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Multidrug resistance protein MdtH {ECO:0000255|HAMAP-Rule:MF_01529};
GN Name=mdtH {ECO:0000255|HAMAP-Rule:MF_01529};
GN OrderedLocusNames=SF1071, S1149;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42693.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP16580.1; -; Genomic_DNA.
DR RefSeq; NP_706986.2; NC_004337.2.
DR RefSeq; WP_000092218.1; NZ_WPGW01000001.1.
DR AlphaFoldDB; Q83LI8; -.
DR SMR; Q83LI8; -.
DR STRING; 198214.SF1071; -.
DR EnsemblBacteria; AAN42693; AAN42693; SF1071.
DR EnsemblBacteria; AAP16580; AAP16580; S1149.
DR GeneID; 1024021; -.
DR KEGG; sfl:SF1071; -.
DR KEGG; sfx:S1149; -.
DR PATRIC; fig|198214.7.peg.1254; -.
DR HOGENOM; CLU_001265_60_2_6; -.
DR OMA; TVCVWTL; -.
DR OrthoDB; 1452500at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..402
FT /note="Multidrug resistance protein MdtH"
FT /id="PRO_0000173351"
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; 44393 MW; 18E0F06849012BB1 CRC64;
MSRVSQARNL GKYFLLIDNM LVVLGFFVVF PLISIRFVDQ MGWAAVMVGI ALGLRQFIQQ
GLGIFGGAIA DRFGAKPMIV TGMLMRAAGF ATMGIAHEPW LLWFSCLLSG LGGTLFDPPR
SALVVKLIRP QQRGRFFSLL MMQDSASAVI GALLGSWLLQ YDFRLVCATG AVLFVLCAAF
NAWLLPAWKL STVRTPVREG MTRVMRDKRF VTYVLTLAGY YMLAVQVMLM LPIMVNDVAG
APSAVKWMYA IEACLSLTLL YPIARWSEKH FRLEHRLMAG LLIMSLSMMP VGMVSGLQQL
FTLICLFYIG SIIAEPARET LSASLADARA RGSYMGFSRL GLAIGGAIGY IGGGWLFDLG
KSAHQPELPW MMLGIIGIFT FLALGWQFSQ KRAARRLLER DA
