ID   SSTT_PSEPG              Reviewed;         403 AA.
AC   B0KLP3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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};
GN   OrderedLocusNames=PputGB1_3530;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000926; ABY99421.1; -; Genomic_DNA.
DR   RefSeq; WP_012273141.1; NC_010322.1.
DR   AlphaFoldDB; B0KLP3; -.
DR   SMR; B0KLP3; -.
DR   STRING; 76869.PputGB1_3530; -.
DR   EnsemblBacteria; ABY99421; ABY99421; PputGB1_3530.
DR   KEGG; ppg:PputGB1_3530; -.
DR   eggNOG; COG3633; Bacteria.
DR   HOGENOM; CLU_044581_0_0_6; -.
DR   OMA; PVNLQLC; -.
DR   Proteomes; UP000002157; 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 inner membrane; Cell membrane; Membrane;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..403
FT                   /note="Serine/threonine transporter SstT"
FT                   /id="PRO_1000087936"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        79..99
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        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
SQ   SEQUENCE   403 AA;  41962 MW;  64DB3E37B61AB662 CRC64;
     MTPLLRFLNR TSLVTQIVIG LLAGIALALL APAIACDLAF LGKVFVSALK AVAPVLVFIL
     VMASIANHRH GQETHIRPIL WLYLLGTFAA AVVAVVASML FPSHLVLSTG EATLSAPGGI
     TEVMQNLVLS AVDNPVNALL NANFIGILTW AIGLGVALRH AGETTRTVVD DLSNGVTLIV
     RMVIRFAPLG IFGLVSSTLA QSGLNALLGY LHLLAVLIGC MLFVALVMNP LIVFWKIRRN
     PYPLTLLCLR ESGITAFFTR SSAANIPVNL ALSERLGLHE DTYSVSIPLG ATINMAGAAI
     TITVLTLAAV HTLGIPVDLP TAVLLSVVAA VCACGASGVA GGSLLLIPLA CSLFGIPSEI
     AMQVVAVGFI IGVLQDSAET ALNSSTDVLF TAAACLAEER RNP