ID   GLTT_BACCA              Reviewed;         421 AA.
AC   P24944;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Proton/sodium-glutamate symport protein;
DE   AltName: Full=Glutamate-aspartate carrier protein;
GN   Name=gltT;
OS   Bacillus caldotenax.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1359385; DOI=10.1111/j.1365-2958.1992.tb01464.x;
RA   Tolner B., Poolman B., Konings W.N.;
RT   "Characterization and functional expression in Escherichia coli of the
RT   sodium/proton/glutamate symport proteins of Bacillus stearothermophilus and
RT   Bacillus caldotenax.";
RL   Mol. Microbiol. 6:2845-2856(1992).
RN   [2]
RP   FUNCTION.
RX   PubMed=8596452; DOI=10.1111/j.1365-2958.1995.mmi_18010123.x;
RA   Tolner B., Ubbink-Kok T., Poolman B., Konings W.N.;
RT   "Cation-selectivity of the L-glutamate transporters of Escherichia coli,
RT   Bacillus stearothermophilus and Bacillus caldotenax: dependence on the
RT   environment in which the proteins are expressed.";
RL   Mol. Microbiol. 18:123-133(1995).
RN   [3]
RP   SUBUNIT.
RX   PubMed=14596613; DOI=10.1021/bi030161q;
RA   Yernool D., Boudker O., Folta-Stogniew E., Gouaux E.;
RT   "Trimeric subunit stoichiometry of the glutamate transporters from Bacillus
RT   caldotenax and Bacillus stearothermophilus.";
RL   Biochemistry 42:12981-12988(2003).
CC   -!- FUNCTION: This carrier protein is part of the Na(+)-dependent, binding-
CC       protein-independent glutamate-aspartate transport system.
CC       {ECO:0000269|PubMed:8596452}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:14596613}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC       (DAACS) (TC 2.A.23) family. {ECO:0000305}.
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DR   EMBL; M86509; AAA22493.1; -; Genomic_DNA.
DR   PIR; S26246; S26246.
DR   AlphaFoldDB; P24944; -.
DR   SMR; P24944; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0046942; P:carboxylic acid transport; IEA:UniProt.
DR   Gene3D; 1.10.3860.10; -; 1.
DR   InterPro; IPR001991; Na-dicarboxylate_symporter.
DR   InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR   InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR   PANTHER; PTHR42865; PTHR42865; 1.
DR   Pfam; PF00375; SDF; 1.
DR   SUPFAM; SSF118215; SSF118215; 1.
DR   PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR   PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..421
FT                   /note="Proton/sodium-glutamate symport protein"
FT                   /id="PRO_0000202086"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..43
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        99..148
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..198
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..222
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..306
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        328..330
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        373..421
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   421 AA;  45345 MW;  10ABBE12EDD1E7E4 CRC64;
     MRKIGLAWQI FIGLILGIIV GAIFYGNPKV AAYLQPIGDI FLRLIKMIVI PIVISSLVVG
     VASVGDLKKL GKLGGKTIIY FEIITTIAIV VGLLAANIFQ PGAGVNMKSL EKTDIQSYVD
     TTNEVQHHSM VETFVNIVPK NIFESLSTGD MLPIIFFSVM FGLGVAAIGE KGKPVLQFFQ
     GTAEAMFYVT NQIMKFAPFG VFALIGVTVS KFGVESLIPL SKLVIVVYAT MLFFIFAVLG
     GVAKLFGINI FHIIKILKDE LILAYSTASS ETVLPRIMDK MEKFGCPKAI TSFVIPTGYS
     FNLDGSTLYQ ALAAIFIAQL YGIDMSVSQQ ISLLLVLMVT SKGIAGVPGV SFVVLLATLG
     TVGIPVEGLA FIAGIDRILD MARTAVNVIG NSLAAIIMSK WEGQYNEEKG KQYLAELQQS
     A