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}.
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; 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
//