SSTT_STRP1
ID SSTT_STRP1 Reviewed; 404 AA.
AC Q9A1E0; Q490S4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 130.
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=SPy_0324, M5005_Spy0275;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(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 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}.
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DR EMBL; AE004092; AAK33382.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ50894.1; -; Genomic_DNA.
DR RefSeq; NP_268661.1; NC_002737.2.
DR AlphaFoldDB; Q9A1E0; -.
DR SMR; Q9A1E0; -.
DR STRING; 1314.HKU360_00314; -.
DR PaxDb; Q9A1E0; -.
DR EnsemblBacteria; AAK33382; AAK33382; SPy_0324.
DR KEGG; spy:SPy_0324; -.
DR KEGG; spz:M5005_Spy0275; -.
DR PATRIC; fig|160490.10.peg.282; -.
DR HOGENOM; CLU_044581_0_0_9; -.
DR OMA; PVNLQLC; -.
DR Proteomes; UP000000750; 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; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..404
FT /note="Serine/threonine transporter SstT"
FT /id="PRO_0000309137"
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; 42554 MW; 5666B970A58A3D07 CRC64;
MKKIYDLWVR VSLIKKIGIG VVIGVMLGIL APDLTGFSIL GKLFVGGLKA IAPLLVFALV
SQAISHQKKG KQTNMTLIIV LYLFGTFASA LVAVLTAYLF PLTLVLNTPV NTELSPPQGV
AEVFQSLLLK LVDNPINALA TANYIGVLSW AIIFGLALKA ASKETKHLIK TAAEVTSQIV
VWIINLAPIG IMSLVFTTIS ENGVGILSDY AFLILVLVGT MLFVALVVNP LIAVLITRQN
PYPLVLRCLR ESGLTAFFTR SSAANIPVNM QLCQKIGLSK DTYSVSIPLG ATINMGGAAI
TINVLTLAAV HTFGIPIDFL TALLLSVVAA VSACGASGVA GGSLLLIPVA CSLFGISNDL
AMQVVGVGFI VGVIQDSCET ALNSSTDVLF TAIAENAFWK RKKA
