SSTT_SHEON
ID SSTT_SHEON Reviewed; 408 AA.
AC Q8ECL5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SO_3122;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014299; AAN56127.1; -; Genomic_DNA.
DR RefSeq; NP_718683.1; NC_004347.2.
DR RefSeq; WP_011073018.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8ECL5; -.
DR SMR; Q8ECL5; -.
DR STRING; 211586.SO_3122; -.
DR PaxDb; Q8ECL5; -.
DR KEGG; son:SO_3122; -.
DR PATRIC; fig|211586.12.peg.3022; -.
DR eggNOG; COG3633; Bacteria.
DR HOGENOM; CLU_044581_0_0_6; -.
DR OMA; PVNLQLC; -.
DR OrthoDB; 781228at2; -.
DR PhylomeDB; Q8ECL5; -.
DR BioCyc; SONE211586:G1GMP-2893-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005295; F:neutral amino acid:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0032329; P:serine transport; IBA:GO_Central.
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..408
FT /note="Serine/threonine transporter SstT"
FT /id="PRO_0000309124"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 43..63
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 192..212
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 316..336
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
SQ SEQUENCE 408 AA; 42173 MW; 648B9B07511E3872 CRC64;
MKQESSFLAK LANGSLVLQI LVGIIAGVAL ASFSHEWAKQ VAFLGSLFVG ALKAIAPILV
FILVASSIAN QKKNTQTNMR PIVVLYLLGT FAAALTAVIL SMMFPTTLVL AAGVEGTSPP
QGISEVISTL LFKLVDNPVN ALMTGNYIGI LAWGVGLGLA LHHSSDSTKQ VFADVSHGIS
QMVHFIIRLA PIGIFGLVAA TFAETGFAAI AGYAQLLAVL LGAMAFIALI INPLIVYVKI
KRNPYPLVIR CLRESGMTAF FTRSSAANIP VNMALCEKLK LHEDTYAVSI PLGATINMGG
AAITITVLTL AAAHTLGIQV DLLTALLLSV VAAISACGAS GVAGGSLLLI PLACSLFGIS
NDVAMQVVAV GFIIGVIQDA AETALNSSTD VIFTAAACEA AENKAKLG