ID   SSTT_ALIF1              Reviewed;         413 AA.
AC   Q5DZC3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=VF_A0803;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000021; AAW87873.1; -; Genomic_DNA.
DR   RefSeq; WP_011263624.1; NC_006841.2.
DR   RefSeq; YP_206761.1; NC_006841.2.
DR   AlphaFoldDB; Q5DZC3; -.
DR   SMR; Q5DZC3; -.
DR   STRING; 312309.VF_A0803; -.
DR   EnsemblBacteria; AAW87873; AAW87873; VF_A0803.
DR   KEGG; vfi:VF_A0803; -.
DR   PATRIC; fig|312309.11.peg.3405; -.
DR   eggNOG; COG3633; Bacteria.
DR   HOGENOM; CLU_044581_0_0_6; -.
DR   OMA; PVNLQLC; -.
DR   OrthoDB; 781228at2; -.
DR   Proteomes; UP000000537; Chromosome II.
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 inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..413
FT                   /note="Serine/threonine transporter SstT"
FT                   /id="PRO_0000309153"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
SQ   SEQUENCE   413 AA;  42943 MW;  6D65A20CE8E4B50C CRC64;
     MSQAQPLLVR MMNTNIVIQI LIGIIAGVAL ATLAPNLAIS AGLFGELFVS ALKAVAPILV
     FILVAASIAN QKRGQNSNMK PVIVLYLVGT FCASLTAVVM SFLFPTTLTL VIDAATNTAP
     EGIVEVINTL LFKIIDNPIN ALMTGNFIGI LGWAVALGLG LHSASDATKK IFVDLSNCIS
     AIVTVVIRFA PIGIFGLVSH TFAETGFAVL AGYSHLLAVL LGSMAFIALI VNPLIVYIRT
     RRNPYPLVFL CLRESGVTAF FTRSSAANIP VNMALCERLN LHKDTYSVSI PLGATINMAG
     AAITITVLTL AAVNTAGVEV DLATALLLSL VAAVSACGAS GVAGGSLLLI PLACSLFGIS
     NDIAMQVVAI GFIIGVVQDS AETALNSSTD VLFTTAACRK ADNPYKPLVQ PTN