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Database: UniProt
Entry: C7BL39_PHOAA
LinkDB: C7BL39_PHOAA
Original site: C7BL39_PHOAA 
ID   C7BL39_PHOAA            Unreviewed;       417 AA.
AC   C7BL39;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 80.
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=ygjU {ECO:0000313|EMBL:CAQ85714.1};
GN   Synonyms=sstT {ECO:0000256|HAMAP-Rule:MF_01582};
GN   OrderedLocusNames=PAU_03626 {ECO:0000313|EMBL:CAQ85714.1};
OS   Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
OS   (Xenorhabdus luminescens (strain 2)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=553480 {ECO:0000313|EMBL:CAQ85714.1, ECO:0000313|Proteomes:UP000002747};
RN   [1] {ECO:0000313|EMBL:CAQ85714.1, ECO:0000313|Proteomes:UP000002747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43949 / 3105-77 {ECO:0000313|Proteomes:UP000002747};
RX   PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA   Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA   Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA   Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA   Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.;
RT   "Comparative genomics of the emerging human pathogen Photorhabdus
RT   asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL   BMC Genomics 10:302-302(2009).
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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01582}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01582}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {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}.
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DR   EMBL; FM162591; CAQ85714.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7BL39; -.
DR   STRING; 291112.PAU_03626; -.
DR   KEGG; pay:PAU_03626; -.
DR   eggNOG; COG3633; Bacteria.
DR   OMA; VIRCAPL; -.
DR   Proteomes; UP000002747; Chromosome.
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; 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}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01582};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01582};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01582};
KW   Symport {ECO:0000256|HAMAP-Rule:MF_01582};
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        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        86..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        215..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT   TRANSMEM        289..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"
SQ   SEQUENCE   417 AA;  44193 MW;  24EF0D197CA1C9B3 CRC64;
     MEKLKSGFVH YITQGSLVKQ ILIGLVAGIL LAWLAPSVAK SVSLLGTLFV GALKAVAPIL
     VWVLVMSSIA NHKKGQKTNI RPILILYILG TFSAALVAVV GSFMFPLQLI LAVNDAQMSP
     PENIMEVMKG MLMNVVANPV NALLNGNYIG ILAWAIGLGI ALRHATDSTK SLIHDMSEAV
     TQVVRVVIRF APIGIFGLVS STIAETGFKT LLGYVYLLVV LLGCMLVMAL VVNPLIVYWK
     IRRNPYPLVF ACLRESGVTA FFTRSSAANI PVNMAMCRRM NLHEDTYSVS IPLGATINME
     GAAVTITVLT LAAVNTLGMP VELLTALLLS VVAAICACGA SGVAGGSLLL IPLACSMFGI
     SNEIAMQVVA VGFIIGVLQD SAETGLNSST DVLFTAAVCQ AEDDRLTSES DQLTRRS
//
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