GLTT_GEOSE
ID GLTT_GEOSE Reviewed; 421 AA.
AC P24943;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Proton/sodium-glutamate symport protein;
DE AltName: Full=Glutamate-aspartate carrier protein;
GN Name=gltT;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
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.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
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 FUNCTION.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=8634258; DOI=10.1021/bi953005v;
RA Gaillard I., Slotboom D.J., Knol J., Lolkema J.S., Konings W.N.;
RT "Purification and reconstitution of the glutamate carrier GltT of the
RT thermophilic bacterium Bacillus stearothermophilus.";
RL Biochemistry 35:6150-6156(1996).
RN [4]
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, ECO:0000269|PubMed:8634258}.
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; M86508; AAA22492.1; -; Genomic_DNA.
DR PIR; S26247; S26247.
DR AlphaFoldDB; P24943; -.
DR SMR; P24943; -.
DR TCDB; 2.A.23.1.2; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
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_0000202085"
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; 45469 MW; 30C5738E8FD3A54F CRC64;
MRKIGLAWQI FIGLILGIIV GAIFYGNPKV ATYLQPIGDI FLRLIKMIVI PIVISSLVVG
VASVGDLKKL GKLGGKTIIY FEIITTIAIV VGLLAANIFQ PGTGVNMKSL EKTDIQSYVD
TTNEVQHHSM VETFVNIVPK NIFESLTKGD MLPIIFFSVM FGLGVAAIGE KGKPVLQFFQ
GTAEAMFYVT NQIMKFAPFG VFALIGVTVS KFGVESLIPL SKLVIVVYAT MVFFIFVVLG
GVAKLFGINI FHIIKILKDE LILAYSTASS ETVLPKIMEK MENFGCPKAI TSFVIPTGYS
FNLDGSTLYQ ALAAIFIAQL YGIDMPISQQ ISLLLVLMVT SKGIAGVPGV SFVVLLATLG
TVGIPIEGLA FIAGIDRILD MARTAVNVIG NSLAAIIMSK WEGQYNEEKG KQYIAQLQQS
A
