ID   SSTT_SALPA              Reviewed;         414 AA.
AC   Q5PCA7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Serine/threonine transporter SstT {ECO:0000255|HAMAP-Rule:MF_01582};
DE   AltName: Full=Na(+)/serine-threonine symporter {ECO:0000255|HAMAP-Rule:MF_01582};
GN   Name=sstT {ECO:0000255|HAMAP-Rule:MF_01582}; OrderedLocusNames=SPA3094;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- FUNCTION: Involved in the import of serine and threonine into the cell,
CC       with the concomitant import of sodium (symport system).
CC       {ECO:0000255|HAMAP-Rule:MF_01582}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01582};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29577;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01582};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine(in) + Na(+)(in) = L-threonine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:69999, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01582};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70001;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01582};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01582}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01582}.
CC   -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC       (DAACS) (TC 2.A.23) family. {ECO:0000255|HAMAP-Rule:MF_01582}.
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DR   EMBL; CP000026; AAV78927.1; -; Genomic_DNA.
DR   RefSeq; WP_000235363.1; NC_006511.1.
DR   AlphaFoldDB; Q5PCA7; -.
DR   SMR; Q5PCA7; -.
DR   EnsemblBacteria; AAV78927; AAV78927; SPA3094.
DR   KEGG; spt:SPA3094; -.
DR   HOGENOM; CLU_044581_0_0_6; -.
DR   OMA; PVNLQLC; -.
DR   Proteomes; UP000008185; 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:0015171; F:amino acid transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032329; P:serine transport; IEA:InterPro.
DR   GO; GO:0015826; P:threonine transport; IEA:InterPro.
DR   Gene3D; 1.10.3860.10; -; 1.
DR   HAMAP; MF_01582; Ser_Thr_transp_SstT; 1.
DR   InterPro; IPR001991; Na-dicarboxylate_symporter.
DR   InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR   InterPro; IPR023025; Ser_Thr_transp_SstT.
DR   PANTHER; PTHR42865; PTHR42865; 1.
DR   Pfam; PF00375; SDF; 1.
DR   SUPFAM; SSF118215; SSF118215; 1.
DR   PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..414
FT                   /note="Serine/threonine transporter SstT"
FT                   /id="PRO_0000309117"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
SQ   SEQUENCE   414 AA;  43413 MW;  2F82B23A5779EB5E CRC64;
     MATQRASGLL QRLAQGSLVK QILVGLVLGI LLAWISKPAA EAVGLLGTLF VGALKAVAPV
     LVLMLVMASI ANHQHGQKTN IRPILFLYLL GTFSAALAAV VFSFAFPSTL HLSSSAQDIV
     PPSGIVEVLR GLLMSMVSNP IDALLNANYI GILVWAVGLG FALRHGNETT KNLVNDMSNA
     VTFMVKLVIR FAPVGIFGLV SSTLATTGFS TLWGYAHLLV VLIGCMLLVA LVVNPLLVFW
     KIRRNPYPLV FACLRESGVY AFFTRSSAAN IPVNMALCEK LNLDRDTYSV SIPLGATINM
     AGAAITITVL TLAAVHTLGV PVDLPTALLL SVVASLCACG ASGVAGGSLL LIPLACNMFG
     IPNDIAMQVV AVGFIIGVLQ DSCETALNSS TDVLFTAAAC QAEDERLANN ALRS