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Database: UniProt
Entry: A0A136WF08_9FIRM
LinkDB: A0A136WF08_9FIRM
Original site: A0A136WF08_9FIRM 
ID   A0A136WF08_9FIRM        Unreviewed;       407 AA.
AC   A0A136WF08;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Serine/threonine transporter SstT {ECO:0000256|HAMAP-Rule:MF_01582};
DE   AltName: Full=Na(+)/serine-threonine symporter {ECO:0000256|HAMAP-Rule:MF_01582};
GN   Name=sstT {ECO:0000256|HAMAP-Rule:MF_01582,
GN   ECO:0000313|EMBL:KXL53070.1};
GN   ORFNames=CLNEO_16130 {ECO:0000313|EMBL:KXL53070.1};
OS   Anaerotignum neopropionicum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerotignum.
OX   NCBI_TaxID=36847 {ECO:0000313|EMBL:KXL53070.1, ECO:0000313|Proteomes:UP000070539};
RN   [1] {ECO:0000313|EMBL:KXL53070.1, ECO:0000313|Proteomes:UP000070539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM-3847 {ECO:0000313|EMBL:KXL53070.1,
RC   ECO:0000313|Proteomes:UP000070539};
RA   Poehlein A., Beck M.H., Bengelsdorf F.R., Daniel R., Duerre P.;
RT   "Genome sequence of Clostridium neopropionicum X4, DSM-3847.";
RL   Submitted (JAN-2016) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01582};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01582};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01582}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC       (DAACS) (TC 2.A.23) family. {ECO:0000256|HAMAP-Rule:MF_01582}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXL53070.1}.
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DR   EMBL; LRVM01000004; KXL53070.1; -; Genomic_DNA.
DR   RefSeq; WP_066087135.1; NZ_LRVM01000004.1.
DR   AlphaFoldDB; A0A136WF08; -.
DR   PATRIC; fig|36847.3.peg.1882; -.
DR   OrthoDB; 9768885at2; -.
DR   Proteomes; UP000070539; Unassembled WGS sequence.
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; Sodium:dicarboxylate symporter; 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; PROTON/GLUTAMATE-ASPARTATE SYMPORTER; 1.
DR   PANTHER; PTHR42865:SF8; SERINE_THREONINE TRANSPORTER SSTT; 1.
DR   Pfam; PF00375; SDF; 1.
DR   PRINTS; PR00173; EDTRNSPORT.
DR   SUPFAM; SSF118215; Proton glutamate symport protein; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport {ECO:0000256|ARBA:ARBA00022970, ECO:0000256|HAMAP-
KW   Rule:MF_01582};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01582};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01582};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070539};
KW   Symport {ECO:0000256|HAMAP-Rule:MF_01582};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01582};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01582};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01582}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        43..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        77..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        135..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        178..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        212..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        295..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        322..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
SQ   SEQUENCE   407 AA;  42458 MW;  432CDB26AFD8B8BE CRC64;
     MNNLFQKWNS ISLVKRIVAG LIIGAVLGRV LPSLTVIGIL GDLFVGALKG VAPILVFFLV
     MSSLAQHKKG AKTNMGTVVV LYLIGTFAAA LVAVVGSFMF PVSLTLTDAV QNSTPPDGVG
     TVIKTLLMNV VQNPIASIST ANYIGILAWA VVFGLALKHS SDTTKTMLGN FADAVSQAVR
     WVISFAPFGI LGLVFATVST SGLGIFTDYG KLLLLLVGCM VVIALIVNPI IVFLNIKQNP
     YPLVFKCLKD SFITAFFTRS SAANIPVNMT LCESLGLDED NYSVSIPLGA TINMAGAAIT
     ITVMTLAAVN TLGFSVDIGT ALVLSIVAAV SACGASGVAG GSLLLIPLAC SLFGISNDIA
     MQVVGVGFII GVVQDSCETG LNSSTDALFT AAAEFRQWRK EGKPIKW
//
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