ID   SSTT_STRP3              Reviewed;         404 AA.
AC   P0DF78; Q878A8; Q8K8K5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 48.
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=SpyM3_0237;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01582};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM78844.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014074; AAM78844.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002991067.1; NC_004070.1.
DR   AlphaFoldDB; P0DF78; -.
DR   SMR; P0DF78; -.
DR   EnsemblBacteria; AAM78844; AAM78844; SpyM3_0237.
DR   KEGG; spg:SpyM3_0237; -.
DR   HOGENOM; CLU_044581_0_0_9; -.
DR   OMA; PVNLQLC; -.
DR   Proteomes; UP000000564; 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.
PE   3: Inferred from homology;
KW   Amino-acid transport; Cell membrane; Membrane; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..404
FT                   /note="Serine/threonine transporter SstT"
FT                   /id="PRO_0000309143"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
SQ   SEQUENCE   404 AA;  42540 MW;  09977196D45CEDBC CRC64;
     MKKIYDLWVR VSLIKKIGIG VVIGVMLGIL APDLTGFSIL GKLFVGGLKA IAPLLVFALV
     SQAISHQKKG KQTNMTLIIV LYLFGTFASA LVAVLTAYLF PLTLVLNTPV NTELSPPQGV
     AEVFQSLLLK LVDNPINALA TANYIGVLSW AIIFGLALKA ASQETKHLIK TAAEVTSQIV
     VWIINLAPIG IMSLVFTTIS ENGVGILSDY AFLILVLVGT MVFVALVVNP LIAVLITRQN
     PYPLVLRCLR ESGLTAFFTR SSAANIPVNM QLCQKIGLSK DTYSVSIPLG ATINMGGAAI
     TINVLTLAAV HTFGIPIDFL TALLLSVVAA VSACGASGVA GGSLLLIPVA CSLFGISNDL
     AMQVVGVGFI VGVIQDSCET ALNSSTDVLF TAIAENAFWK RKKA