SSTT_STRPD
ID SSTT_STRPD Reviewed; 404 AA.
AC Q1JII6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=MGAS10270_Spy0272;
OS Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370552;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10270;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000260; ABF33337.1; -; Genomic_DNA.
DR RefSeq; WP_002991840.1; NC_008022.1.
DR AlphaFoldDB; Q1JII6; -.
DR SMR; Q1JII6; -.
DR EnsemblBacteria; ABF33337; ABF33337; MGAS10270_Spy0272.
DR KEGG; sph:MGAS10270_Spy0272; -.
DR HOGENOM; CLU_044581_0_0_9; -.
DR OMA; PVNLQLC; -.
DR Proteomes; UP000002436; 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_0000309141"
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; 42568 MW; D95C3C6D977719E0 CRC64;
MKKIYDLWVR VSLIKKIGIG VVIGVMLGIL APDLTGFSIL GKLFVGGLKA IAPLLVFALV
SQAISHQKKG RQTNMTLIIV 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