ID A0A0R1YMX2_9LACO Unreviewed; 417 AA.
AC A0A0R1YMX2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=FD40_GL000043 {ECO:0000313|EMBL:KRM43455.1}, LA20533_05895
GN {ECO:0000313|EMBL:APT18818.1};
OS Amylolactobacillus amylophilus DSM 20533 = JCM 1125.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Amylolactobacillus.
OX NCBI_TaxID=1423721 {ECO:0000313|EMBL:KRM43455.1, ECO:0000313|Proteomes:UP000051230};
RN [1] {ECO:0000313|EMBL:KRM43455.1, ECO:0000313|Proteomes:UP000051230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20533 {ECO:0000313|EMBL:KRM43455.1,
RC ECO:0000313|Proteomes:UP000051230};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
RN [2] {ECO:0000313|EMBL:APT18818.1, ECO:0000313|Proteomes:UP000185499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20533 {ECO:0000313|EMBL:APT18818.1,
RC ECO:0000313|Proteomes:UP000185499};
RA Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "The whole genome sequencing and assembly of Lactobacillus amylophilus DSM
RT 20533T strain.";
RL Submitted (DEC-2016) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01582}.
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DR EMBL; CP018888; APT18818.1; -; Genomic_DNA.
DR EMBL; AYYS01000004; KRM43455.1; -; Genomic_DNA.
DR RefSeq; WP_056945806.1; NZ_CP018888.1.
DR AlphaFoldDB; A0A0R1YMX2; -.
DR STRING; 1423721.LA20533_05895; -.
DR KEGG; lah:LA20533_05895; -.
DR PATRIC; fig|1423721.4.peg.42; -.
DR OrthoDB; 9768885at2; -.
DR Proteomes; UP000051230; Unassembled WGS sequence.
DR Proteomes; UP000185499; 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};
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 Reference proteome {ECO:0000313|Proteomes:UP000051230};
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 14..34
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 74..97
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 208..230
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 281..305
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 317..345
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
SQ SEQUENCE 417 AA; 44552 MW; 0A75C8471EF894BB CRC64;
MWATYTRISL IKRIIIGIVI GFVLGLTLPS WTWIGVIGNL FINALKAIAP ILVFFIITAA
LARHKKGSQT NMRSIVILYL GATFVAALVA VLVTYLFPIT VVFPKEAVAG VPKAPKAIGE
VINQLLMNAV ANPVSALMEG NYLSILFWAV LLGLGLRSIG EATKKTVIDL SEAVTHVVQS
IIQMAPFGII GLVFNSVAST GIKGMATYGR LILLLAGTMF FVNFVIYPLM TWLMVRQNPF
PLTWFAFKES GIPAFFTRSS AVNIPINLDL ARRLKLDKNT YSISIPLGGS ANSGGAAITI
SIMTLTAANT LGLHVDFFTA FLLCLLTAIS ATGASGIAGG SLLLIPLSCS LFGISNDIAM
QMVGIGFIIG VIQDAVETAV NSASDLVFTA TAEYAHLRRI GQPVDIVKQV REAKETD
//
