GLTS_ECOLI
ID GLTS_ECOLI Reviewed; 401 AA.
AC P0AER8; P19933; Q2M7W6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Sodium/glutamate symporter {ECO:0000255|HAMAP-Rule:MF_02062, ECO:0000305};
DE AltName: Full=Glutamate permease {ECO:0000303|PubMed:2017136};
GN Name=gltS {ECO:0000255|HAMAP-Rule:MF_02062}; Synonyms=gltC;
GN OrderedLocusNames=b3653, JW3628;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RX PubMed=2254324; DOI=10.1016/s0021-9258(18)45797-3;
RA Deguchi Y., Yamato I., Anraku Y.;
RT "Nucleotide sequence of gltS, the Na+/glutamate symport carrier gene of
RT Escherichia coli B.";
RL J. Biol. Chem. 265:21704-21708(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2017136; DOI=10.1007/bf00261677;
RA Kalman M., Gentry D., Cashel M.;
RT "Characterization of the Escherichia coli K12 gltS glutamate permease
RT gene.";
RL Mol. Gen. Genet. 225:379-386(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 379-401.
RC STRAIN=K12;
RX PubMed=1544582; DOI=10.1016/0378-1119(92)90449-y;
RA Kalman M., Murphy H., Cashel M.;
RT "The nucleotide sequence of recG, the distal spo operon gene in Escherichia
RT coli K-12.";
RL Gene 110:95-99(1992).
RN [7]
RP FUNCTION.
RC STRAIN=D2W;
RX PubMed=336628; DOI=10.1016/s0021-9258(17)38344-8;
RA Schellenberg G.D., Furlong C.E.;
RT "Resolution of the multiplicity of the glutamate and aspartate transport
RT systems of Escherichia coli.";
RL J. Biol. Chem. 252:9055-9064(1977).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=B;
RX PubMed=2537813; DOI=10.1128/jb.171.3.1314-1319.1989;
RA Deguchi Y., Yamato I., Anraku Y.;
RT "Molecular cloning of gltS and gltP, which encode glutamate carriers of
RT Escherichia coli B.";
RL J. Bacteriol. 171:1314-1319(1989).
RN [9]
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 [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [11]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=17269795; DOI=10.1021/bi062275i;
RA Dobrowolski A., Sobczak-Elbourne I., Lolkema J.S.;
RT "Membrane topology prediction by hydropathy profile alignment: membrane
RT topology of the Na(+)-glutamate transporter GltS.";
RL Biochemistry 46:2326-2332(2007).
RN [12]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=17662058; DOI=10.1111/j.1574-6968.2007.00863.x;
RA Szvetnik A., Gal J., Kalman M.;
RT "Membrane topology of the GltS Na+/glutamate permease of Escherichia
RT coli.";
RL FEMS Microbiol. Lett. 275:71-79(2007).
CC -!- FUNCTION: Catalyzes the sodium-dependent, binding-protein-independent
CC transport of glutamate. {ECO:0000255|HAMAP-Rule:MF_02062,
CC ECO:0000269|PubMed:2537813, ECO:0000269|PubMed:336628,
CC ECO:0000269|PubMed:8596452}.
CC -!- ACTIVITY REGULATION: Inhibited by the uncoupler carbonylcyanide m-
CC chlorophenylhydrazone (CCCP) and the ionophore monensin.
CC {ECO:0000269|PubMed:2537813}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=5.2 nmol/min/mg enzyme {ECO:0000269|PubMed:2537813};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02062, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:17269795, ECO:0000269|PubMed:17662058,
CC ECO:0000269|PubMed:2537813}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_02062, ECO:0000269|PubMed:17269795,
CC ECO:0000269|PubMed:17662058}.
CC -!- SIMILARITY: Belongs to the glutamate:Na(+) symporter (ESS) (TC 2.A.27)
CC family. {ECO:0000255|HAMAP-Rule:MF_02062, ECO:0000305}.
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DR EMBL; D00626; BAA00517.1; -; Genomic_DNA.
DR EMBL; X17499; CAA35540.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62006.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76677.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77640.1; -; Genomic_DNA.
DR EMBL; M64367; AAA24514.1; -; Genomic_DNA.
DR PIR; G65166; YOECNQ.
DR RefSeq; NP_418110.1; NC_000913.3.
DR RefSeq; WP_000468833.1; NZ_SSZK01000043.1.
DR AlphaFoldDB; P0AER8; -.
DR BioGRID; 4262574; 14.
DR DIP; DIP-48023N; -.
DR IntAct; P0AER8; 1.
DR STRING; 511145.b3653; -.
DR TCDB; 2.A.27.1.1; the glutamate:na(+) symporter (ess) family.
DR PaxDb; P0AER8; -.
DR PRIDE; P0AER8; -.
DR EnsemblBacteria; AAC76677; AAC76677; b3653.
DR EnsemblBacteria; BAE77640; BAE77640; BAE77640.
DR GeneID; 58389951; -.
DR GeneID; 948166; -.
DR KEGG; ecj:JW3628; -.
DR KEGG; eco:b3653; -.
DR PATRIC; fig|1411691.4.peg.3053; -.
DR EchoBASE; EB0401; -.
DR eggNOG; COG0786; Bacteria.
DR HOGENOM; CLU_040907_0_0_6; -.
DR InParanoid; P0AER8; -.
DR OMA; PTAMVNM; -.
DR PhylomeDB; P0AER8; -.
DR BioCyc; EcoCyc:GLTS-MON; -.
DR BioCyc; MetaCyc:GLTS-MON; -.
DR PRO; PR:P0AER8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015501; F:glutamate:sodium symporter activity; IDA:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IDA:EcoCyc.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IEA:InterPro.
DR HAMAP; MF_02062; GltS; 1.
DR InterPro; IPR004445; GltS.
DR PANTHER; PTHR36178; PTHR36178; 1.
DR Pfam; PF03616; Glt_symporter; 1.
DR TIGRFAMs; TIGR00210; gltS; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Ion transport;
KW Membrane; Reference proteome; Sodium; Sodium transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..401
FT /note="Sodium/glutamate symporter"
FT /id="PRO_0000052332"
FT TOPO_DOM 1..6
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:17269795,
FT ECO:0000305|PubMed:17662058"
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17269795,
FT ECO:0000305|PubMed:17662058"
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..69
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:17269795,
FT ECO:0000305|PubMed:17662058"
FT TRANSMEM 70..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17269795,
FT ECO:0000305|PubMed:17662058"
FT TRANSMEM 94..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..156
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:17269795"
FT TRANSMEM 157..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17269795"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..244
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:17269795,
FT ECO:0000305|PubMed:17662058"
FT TRANSMEM 245..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17269795,
FT ECO:0000305|PubMed:17662058"
FT TRANSMEM 277..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..301
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:17269795,
FT ECO:0000305|PubMed:17662058"
FT TRANSMEM 302..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17269795,
FT ECO:0000305|PubMed:17662058"
FT TRANSMEM 368..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..401
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000305|PubMed:17269795, ECO:0000305|PubMed:17662058"
FT CONFLICT 378
FT /note="G -> S (in Ref. 1; BAA00517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 42425 MW; 9569AE0AF75634EC CRC64;
MFHLDTLATL VAATLTLLLG RKLVHSVSFL KKYTIPEPVA GGLLVALALL VLKKSMGWEV
NFDMSLRDPL MLAFFATIGL NANIASLRAG GRVVGIFLIV VVGLLVMQNA IGIGMASLLG
LDPLMGLLAG SITLSGGHGT GAAWSKLFIE RYGFTNATEV AMACATFGLV LGGLIGGPVA
RYLVKHSTTP NGIPDDQEVP TAFEKPDVGR MITSLVLIET IALIAICLTV GKIVAQLLAG
TAFELPTFVC VLFVGVILSN GLSIMGFYRV FERAVSVLGN VSLSLFLAMA LMGLKLWELA
SLALPMLAIL VVQTIFMALY AIFVTWRMMG KNYDAAVLAA GHCGFGLGAT PTAIANMQAI
TERFGPSHMA FLVVPMVGAF FIDIVNALVI KLYLMLPIFA G
