ID G4CHQ4_9NEIS Unreviewed; 409 AA.
AC G4CHQ4;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 ECO:0000313|EMBL:EGY52633.1};
GN ORFNames=HMPREF9371_1143 {ECO:0000313|EMBL:EGY52633.1};
OS Neisseria shayeganii 871.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1032488 {ECO:0000313|EMBL:EGY52633.1, ECO:0000313|Proteomes:UP000003019};
RN [1] {ECO:0000313|EMBL:EGY52633.1, ECO:0000313|Proteomes:UP000003019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=871 {ECO:0000313|EMBL:EGY52633.1,
RC ECO:0000313|Proteomes:UP000003019};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (MAY-2011) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGY52633.1}.
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DR EMBL; AGAY01000043; EGY52633.1; -; Genomic_DNA.
DR RefSeq; WP_009118836.1; NZ_JH164926.1.
DR AlphaFoldDB; G4CHQ4; -.
DR STRING; 1032488.HMPREF9371_1143; -.
DR PATRIC; fig|1032488.3.peg.1073; -.
DR HOGENOM; CLU_044581_0_0_4; -.
DR OrthoDB; 9768885at2; -.
DR Proteomes; UP000003019; Unassembled WGS sequence.
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:UP000003019};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 86..109
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 145..167
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 222..243
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
FT TRANSMEM 328..356
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01582"
SQ SEQUENCE 409 AA; 42455 MW; 2A1CB0763876FD3C CRC64;
MAKQNWAAAL DRIGLVMQIV IGLILGVLVG WLSRDTGMGG AVGELGQILG GLFVGALKAV
APILIFVLVT AAISQSRSGT ATNMRPILLL YLFGTFAAAL VAVSASFAFP STLTLSGVEA
ATREAPGGIG EVMRNLLMKL VSNPIQALAD ANYIGILAWA LVLGAALRQA GERTRELIAD
LAAAVSTVVR WVIRFAPLGI FGLVLTTIIV EGFSGIGRYV HLLAVLLGAM LFVALVVNPL
IVFAQTRSNP YPLVFTCLRE SGMTAFFTRS SAANIPVNMA LAKKLGLNED TYSVSIPLGA
TINMAGAAIT ITVLTLAAVH TLGIEVDFWT AVLLSVVASL GACGASGVAG GSLLLIPMAC
SLFNIENDIA MQVVAVGFII GVVQDSAETA LNSSTDVLFT AAVDQARRR
//
