ID F3L479_9GAMM Unreviewed; 413 AA.
AC F3L479;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 ORFNames=IMCC3088_2448 {ECO:0000313|EMBL:EGG28851.1};
OS Aequoribacter fuscus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Aequoribacter.
OX NCBI_TaxID=2518989 {ECO:0000313|EMBL:EGG28851.1, ECO:0000313|Proteomes:UP000005615};
RN [1] {ECO:0000313|EMBL:EGG28851.1, ECO:0000313|Proteomes:UP000005615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC3088 {ECO:0000313|EMBL:EGG28851.1,
RC ECO:0000313|Proteomes:UP000005615};
RX PubMed=21551310; DOI=10.1128/JB.05111-11;
RA Jang Y., Oh H.M., Kang I., Lee K., Yang S.J., Cho J.C.;
RT "Genome sequence of strain IMCC3088, a proteorhodopsin-containing marine
RT bacterium belonging to the OM60/NOR5 clade.";
RL J. Bacteriol. 193:3415-3416(2011).
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:EGG28851.1}.
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DR EMBL; AEIG01000077; EGG28851.1; -; Genomic_DNA.
DR RefSeq; WP_009576618.1; NZ_CP036423.1.
DR AlphaFoldDB; F3L479; -.
DR eggNOG; COG3633; Bacteria.
DR Proteomes; UP000005615; 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:UP000005615};
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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 51..75
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 87..110
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 187..212
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 291..318
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 353..382
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
SQ SEQUENCE 413 AA; 42453 MW; F5EB940B08F3E524 CRC64;
MLAVIIALGD VMALFDSKGL VFRIAVGVIV GAVLGLLAPD LGQQVGILGE LFVGLLKAIA
PMLVLVLVTS ALANLQRSQT SRPAISLTLL LYLLGTVGAA VVALLLSVAF PQQLHLLSAV
DGNPPGSVLA VLADVLRRMV DNPIRALIEA NFLACLVWGV LFGLSFRSAP GSLRHGLAAV
SERLTEIVRW IIQLAPLGIF GLVSVTVARV GVDALMDYLN LALLLVAAML VVAFGVNALI
VGLLTRKNPY PLILACLRDS GITAFFTRSS AANIPVNLAL SERLGLPSSL YSVTIPVGAT
INMAGAAITI TVLTLAAVNT LGIEVGLVSS LLLCIVAALA ACGASGVPSG SLLLIPLACG
LFGISADVAM QVVAVGFVIS VVQDSAETAL NSSTDVVFTA TVSERLGLTR EVD
//
