SSTT_ECOK1
ID SSTT_ECOK1 Reviewed; 414 AA.
AC A1AG06;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Serine/threonine transporter SstT {ECO:0000255|HAMAP-Rule:MF_01582};
DE AltName: Full=Na(+)/serine-threonine symporter {ECO:0000255|HAMAP-Rule:MF_01582};
GN Name=sstT {ECO:0000255|HAMAP-Rule:MF_01582}; OrderedLocusNames=Ecok1_31020;
GN ORFNames=APECO1_3330;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
CC -!- FUNCTION: Involved in the import of serine and threonine into the cell,
CC with the concomitant import of sodium (symport system).
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01582};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29577;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01582};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70001;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01582};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01582}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01582}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000255|HAMAP-Rule:MF_01582}.
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DR EMBL; CP000468; ABJ02596.1; -; Genomic_DNA.
DR RefSeq; WP_000211386.1; NC_008563.1.
DR AlphaFoldDB; A1AG06; -.
DR SMR; A1AG06; -.
DR EnsemblBacteria; ABJ02596; ABJ02596; APECO1_3330.
DR KEGG; ecv:APECO1_3330; -.
DR HOGENOM; CLU_044581_0_0_6; -.
DR OMA; PVNLQLC; -.
DR Proteomes; UP000008216; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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; PTHR42865; 1.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT CHAIN 2..414
FT /note="Serine/threonine transporter SstT"
FT /id="PRO_0000309087"
FT TOPO_DOM 2..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TOPO_DOM 37..45
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TOPO_DOM 67..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TOPO_DOM 105..142
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TOPO_DOM 164..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TOPO_DOM 201..217
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TOPO_DOM 239..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TOPO_DOM 321..331
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TOPO_DOM 353..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
SQ SEQUENCE 414 AA; 43440 MW; FDABE4284AE08FDC CRC64;
MTTQHSPGLF RRLAHGSLVK QILAGLILGI LLAWISKPAA EAVGLLGTLF VGALKAVAPI
LVLMLVMASI ANHQHGQKTN IRPILFLYLL GTFSAALAAV IFSFAFPSTL HLSSSAGDIS
PPSGIVEVMR GLVMSMVSNP IDALLKGNYI GILVWAIGLG FALRHGNETT KNLVNDMSNA
VTFMVKLVIH FAPIGIFGLV SSTLATTGFS TLWGYAQLLV VLVGCMLLVA LVVNPLLVWW
KIRRNPFPLV LLCLRESGVY AFFTRSSAAN IPVNMALCEK LNLDRDTYSV SIPLGATINM
AGAAITITVL TLAAVNTLGI PVDLPTALLL SVVASLCACG ASGVAGGSLL LIPLACNMFG
ISNDIAMQVV AVGFIIGVLQ DSCETALNSS TDVLFTAAAC QAEDDRLANS ALRN
