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Database: UniProt
Entry: A0A014LXE2_9GAMM
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ID   A0A014LXE2_9GAMM        Unreviewed;       411 AA.
AC   A0A014LXE2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=BG55_17655 {ECO:0000313|EMBL:EXU74231.1};
OS   Erwinia mallotivora.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU74231.1, ECO:0000313|Proteomes:UP000019918};
RN   [1] {ECO:0000313|EMBL:EXU74231.1, ECO:0000313|Proteomes:UP000019918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU74231.1,
RC   ECO:0000313|Proteomes:UP000019918};
RA   Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA   Mat Amin N.;
RT   "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT   pathogen.";
RL   Submitted (FEB-2014) 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:EXU74231.1}.
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DR   EMBL; JFHN01000063; EXU74231.1; -; Genomic_DNA.
DR   RefSeq; WP_034940018.1; NZ_JFHN01000063.1.
DR   AlphaFoldDB; A0A014LXE2; -.
DR   STRING; 69222.BG55_17655; -.
DR   PATRIC; fig|69222.5.peg.3602; -.
DR   OrthoDB; 9768885at2; -.
DR   Proteomes; UP000019918; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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}; Kinase {ECO:0000313|EMBL:EXU74231.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01582};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019918};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:EXU74231.1};
KW   Symport {ECO:0000256|HAMAP-Rule:MF_01582};
KW   Transferase {ECO:0000313|EMBL:EXU74231.1};
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..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        55..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        84..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        143..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        182..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        217..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        293..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        326..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        357..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
SQ   SEQUENCE   411 AA;  43144 MW;  308A531D3BD42D00 CRC64;
     MEKSRPGLLQ RLLQASLVSQ ILIGLLAGIA LAWFSKESAQ SVGLLGTLFV NALKAVAPML
     VMVLVIASIA NHQHGQKTNI RPIITLYLLS TFFAAVLAVV CSHLLPQSLT LSAVDQQIVP
     PSGIMAVLNG LLMSMISNPV DALLHANYIG ILVWAIGLGF AFRHSSQTTR TFLNDAADAI
     TWLVRIVIRF APLGIFGLVG SILASTGFSA LWNYAHLLGL LIGCMLLMAL VVNPVLVLWK
     IRRNPYPLVF TCLRESGVTA FFTRSSAANI PVNMALAKKL GLDEDTYSVS IPVGANISMA
     GAAITITVLT LAAVNTLGIH VDISTAILLS VVASICACGA SGVAGGSLLL IPVACNMFGI
     PADVAMQVVA VGFIIGVLQD SAETALNSSA DILFTAAACM AEQQAEQQRT S
//
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