SSTT_NEIMB
ID SSTT_NEIMB Reviewed; 409 AA.
AC Q9JXB8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=NMB2133;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE002098; AAF42441.1; -; Genomic_DNA.
DR PIR; F81003; F81003.
DR RefSeq; NP_275118.1; NC_003112.2.
DR RefSeq; WP_002225733.1; NC_003112.2.
DR AlphaFoldDB; Q9JXB8; -.
DR SMR; Q9JXB8; -.
DR PaxDb; Q9JXB8; -.
DR EnsemblBacteria; AAF42441; AAF42441; NMB2133.
DR KEGG; nme:NMB2133; -.
DR PATRIC; fig|122586.8.peg.2718; -.
DR HOGENOM; CLU_044581_0_0_4; -.
DR OMA; PVNLQLC; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005295; F:neutral amino acid:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0032329; P:serine transport; IBA:GO_Central.
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.
PE 3: Inferred from homology;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..409
FT /note="Serine/threonine transporter SstT"
FT /id="PRO_0000309101"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01582"
SQ SEQUENCE 409 AA; 41942 MW; 1A7BB589E9A5B58F CRC64;
MAFGKSLFHA IGRVSLVRQI AAGLALGIVI GSVSPQLGLA AGLFGSLFVG ALKAVAPVLV
FILVAATIAQ HQKGNKAHIR PIIVLYLIGT FSAALTAVIA GMVFPTHIVL AGAGDVSAAP
PSGIVEVLKS LLMNLVANPI NAIANANYIG ILAWALVLGA ALRNHGSDVT RQVVADLAEA
VSTVVKWIIR FAPLGIFGLV SSTIAETGFG ALAGYAKLLA VLLGCMAFIA LAVNPAIVWW
KIRRNPFPLV FTCLRESGVY AFFTRSSAAN IPVNMALAKK LGLHEDTYSI SIPLGATINM
AGAAITITVL AMAAAHTQGI TVDFATALLL SLVATVSACG ASGVAGGSLL LIPLACSLFG
IDNDVAMQVV AVGFIIGVIQ DSAETALNSS TDVLFTAAAD LGRQRNRAE