SSTT_ECOLI
ID SSTT_ECOLI Reviewed; 414 AA.
AC P0AGE4; P42602; Q2M9B7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Serine/threonine transporter SstT;
DE AltName: Full=Na(+)/serine-threonine symporter;
GN Name=sstT {ECO:0000303|PubMed:9852024}; Synonyms=ygjU;
GN OrderedLocusNames=b3089, JW3060;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / W3133;
RX PubMed=12097162; DOI=10.1093/oxfordjournals.jbchem.a003201;
RA Kim Y.-M., Ogawa W., Tamai E., Kuroda T., Mizushima T., Tsuchiya T.;
RT "Purification, reconstitution, and characterization of Na(+)/serine
RT symporter, SstT, of Escherichia coli.";
RL J. Biochem. 132:71-76(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 268-414.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Mizobuchi K.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=K12 / W3133;
RX PubMed=9852024; DOI=10.1128/jb.180.24.6749-6752.1998;
RA Ogawa W., Kim Y.-M., Mizushima T., Tsuchiya T.;
RT "Cloning and expression of the gene for the Na+-coupled serine transporter
RT from Escherichia coli and characteristics of the transporter.";
RL J. Bacteriol. 180:6749-6752(1998).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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, ECO:0000269|PubMed:12097162,
CC ECO:0000269|PubMed:9852024}.
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 ECO:0000269|PubMed:12097162, ECO:0000269|PubMed:9852024};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29577;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01582,
CC ECO:0000269|PubMed:12097162, ECO:0000269|PubMed:9852024};
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 ECO:0000269|PubMed:12097162, ECO:0000269|PubMed:9852024};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70001;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01582,
CC ECO:0000269|PubMed:12097162, ECO:0000269|PubMed:9852024};
CC -!- ACTIVITY REGULATION: Activated by valinomycin and inhibited by
CC monensin. {ECO:0000269|PubMed:12097162}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.82 uM for serine {ECO:0000269|PubMed:12097162};
CC Vmax=0.37 umol/min/mg enzyme {ECO:0000269|PubMed:12097162};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:12097162};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:12097162};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01582, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01582}.
CC -!- INDUCTION: Repressed by tryptophan. {ECO:0000269|PubMed:9852024}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000255|HAMAP-Rule:MF_01582,
CC ECO:0000305}.
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DR EMBL; U18997; AAA57891.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76124.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77139.1; -; Genomic_DNA.
DR EMBL; D13328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; F65097; F65097.
DR RefSeq; NP_417560.1; NC_000913.3.
DR RefSeq; WP_000211655.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P0AGE4; -.
DR SMR; P0AGE4; -.
DR BioGRID; 4260951; 17.
DR STRING; 511145.b3089; -.
DR TCDB; 2.A.23.1.13; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR PaxDb; P0AGE4; -.
DR PRIDE; P0AGE4; -.
DR EnsemblBacteria; AAC76124; AAC76124; b3089.
DR EnsemblBacteria; BAE77139; BAE77139; BAE77139.
DR GeneID; 66673012; -.
DR GeneID; 947605; -.
DR KEGG; ecj:JW3060; -.
DR KEGG; eco:b3089; -.
DR PATRIC; fig|1411691.4.peg.3640; -.
DR EchoBASE; EB2590; -.
DR eggNOG; COG3633; Bacteria.
DR HOGENOM; CLU_044581_0_0_6; -.
DR InParanoid; P0AGE4; -.
DR OMA; PVNLQLC; -.
DR PhylomeDB; P0AGE4; -.
DR BioCyc; EcoCyc:YGJU-MON; -.
DR BioCyc; MetaCyc:YGJU-MON; -.
DR PRO; PR:P0AGE4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:EcoliWiki.
DR GO; GO:0005295; F:neutral amino acid:sodium symporter activity; IDA:EcoliWiki.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IDA:EcoliWiki.
DR GO; GO:0032329; P:serine transport; IDA:EcoliWiki.
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 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582,
FT ECO:0000269|PubMed:12097162"
FT CHAIN 2..414
FT /note="Serine/threonine transporter SstT"
FT /id="PRO_0000202118"
FT TOPO_DOM 2..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..45
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..142
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..217
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..331
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 414 AA; 43478 MW; 47713C1DB77B1E38 CRC64;
MTTQRSPGLF RRLAHGSLVK QILVGLVLGI LLAWISKPAA EAVGLLGTLF VGALKAVAPI
LVLMLVMASI ANHQHGQKTN IRPILFLYLL GTFSAALAAV VFSFAFPSTL HLSSSAGDIS
PPSGIVEVMR GLVMSMVSNP IDALLKGNYI GILVWAIGLG FALRHGNETT KNLVNDMSNA
VTFMVKLVIR FAPIGIFGLV SSTLATTGFS TLWGYAQLLV VLVGCMLLVA LVVNPLLVWW
KIRRNPFPLV LLCLRESGVY AFFTRSSAAN IPVNMALCEK LNLDRDTYSV SIPLGATINM
AGAAITITVL TLAAVNTLGI PVDLPTALLL SVVASLCACG ASGVAGGSLL LIPLACNMFG
ISNDIAMQVV AVGFIIGVLQ DSCETALNSS TDVLFTAAAC QAEDDRLANS ALRN
