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
//