ID   MDTI_SHIFL              Reviewed;         109 AA.
AC   Q83RD1; Q7C1H9;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Spermidine export protein MdtI;
GN   Name=mdtI; OrderedLocusNames=SF1620, S1752;
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   -!- FUNCTION: Catalyzes the excretion of spermidine. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with MdtJ. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the drug/metabolite transporter (DMT)
CC       superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. MdtI
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01597}.
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DR   EMBL; AE005674; AAN43203.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17091.1; -; Genomic_DNA.
DR   RefSeq; NP_707496.1; NC_004337.2.
DR   RefSeq; WP_000046666.1; NZ_WPGW01000024.1.
DR   AlphaFoldDB; Q83RD1; -.
DR   SMR; Q83RD1; -.
DR   STRING; 198214.SF1620; -.
DR   EnsemblBacteria; AAN43203; AAN43203; SF1620.
DR   EnsemblBacteria; AAP17091; AAP17091; S1752.
DR   GeneID; 1024848; -.
DR   KEGG; sfl:SF1620; -.
DR   KEGG; sft:NCTC1_01758; -.
DR   KEGG; sfx:S1752; -.
DR   PATRIC; fig|198214.7.peg.1914; -.
DR   HOGENOM; CLU_133067_0_4_6; -.
DR   OMA; VAAGWIM; -.
DR   OrthoDB; 1921902at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0015606; F:spermidine transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR   HAMAP; MF_01597; MdtI; 1.
DR   InterPro; IPR000390; Small_drug/metabolite_transptr.
DR   InterPro; IPR045324; Small_multidrug_res.
DR   InterPro; IPR023737; Spermidine_export_MdtI.
DR   PANTHER; PTHR30561; PTHR30561; 1.
DR   PANTHER; PTHR30561:SF6; PTHR30561:SF6; 1.
DR   Pfam; PF00893; Multi_Drug_Res; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..109
FT                   /note="Spermidine export protein MdtI"
FT                   /id="PRO_0000108078"
FT   TOPO_DOM        1..5
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..63
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   109 AA;  11748 MW;  998F61985CA40C1D CRC64;
     MAQFEWVHAA WLALAIVLEI VANVFLKFSD GFRRKIFGLL SLAAVLAAFS ALSQAVKGID
     LSVVYALWGG FGIAATLAAG WILFGQRLNR KGWIGLVLLL AGMIMVKLA