(data stored in SCRATCH zone)

SWISSPROT: GLTP_BACSU

ID   GLTP_BACSU              Reviewed;         414 AA.
AC   P39817;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   11-DEC-2019, entry version 125.
DE   RecName: Full=Proton/glutamate-aspartate symporter {ECO:0000305};
DE   AltName: Full=Proton/glutamate symport protein {ECO:0000303|PubMed:7751298};
GN   Name=gltP {ECO:0000303|PubMed:7751298}; OrderedLocusNames=BSU02340;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=168 / 6GM;
RX   PubMed=7751298; DOI=10.1128/jb.177.10.2863-2869.1995;
RA   Tolner B., Ubbink-Kok T., Poolman B., Konings W.N.;
RT   "Characterization of the proton/glutamate symport protein of Bacillus
RT   subtilis and its functional expression in Escherichia coli.";
RL   J. Bacteriol. 177:2863-2869(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT   "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT   Bacillus subtilis chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Catalyzes the proton-dependent, binding-protein-independent
CC       transport of glutamate and aspartate. {ECO:0000269|PubMed:7751298}.
CC   -!- ACTIVITY REGULATION: Glutamate uptake is inhibited by beta-
CC       hydroxyaspartate and cysteic acid. {ECO:0000269|PubMed:7751298}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9 uM for glutamate {ECO:0000269|PubMed:7751298};
CC         Vmax=65 nmol/min/mg enzyme with glutamate as substrate
CC         {ECO:0000269|PubMed:7751298};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7751298};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC       (DAACS) (TC 2.A.23) family. {ECO:0000305}.
DR   EMBL; U15147; AAA82878.1; -; Genomic_DNA.
DR   EMBL; AB006424; BAA33131.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12028.1; -; Genomic_DNA.
DR   PIR; B57142; B57142.
DR   RefSeq; NP_388116.1; NC_000964.3.
DR   RefSeq; WP_003234847.1; NZ_JNCM01000030.1.
DR   SMR; P39817; -.
DR   STRING; 224308.BSU02340; -.
DR   PaxDb; P39817; -.
DR   PRIDE; P39817; -.
DR   EnsemblBacteria; CAB12028; CAB12028; BSU02340.
DR   GeneID; 938421; -.
DR   KEGG; bsu:BSU02340; -.
DR   PATRIC; fig|224308.179.peg.240; -.
DR   eggNOG; COG1301; LUCA.
DR   HOGENOM; HOG000208778; -.
DR   InParanoid; P39817; -.
DR   KO; K11102; -.
DR   OMA; QYKTQYS; -.
DR   PhylomeDB; P39817; -.
DR   BioCyc; BSUB:BSU02340-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015810; P:aspartate transmembrane transport; IEA:InterPro.
DR   GO; GO:0006835; P:dicarboxylic acid transport; IBA:GO_Central.
DR   GO; GO:0015813; P:L-glutamate transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.10.3860.10; -; 1.
DR   InterPro; IPR033380; GltP/GltT.
DR   InterPro; IPR001991; Na-dicarboxylate_symporter.
DR   InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR   InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR   PANTHER; PTHR42865:SF4; PTHR42865:SF4; 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;
DR   PRODOM; P39817.
DR   SWISS-2DPAGE; P39817.
KW   Amino-acid transport; Cell membrane; Membrane; Reference proteome; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..414
FT                   /note="Proton/glutamate-aspartate symporter"
FT                   /id="PRO_0000202087"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..42
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..73
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..144
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..182
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..219
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..300
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        322..324
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        325..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        367..414
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   414 AA;  44615 MW;  BFF9008FBA4A5298 CRC64;
     MKKLIAFQIL IALAVGAVIG HFFPDFGMAL RPVGDGFIRL IKMIVVPIVF STIVIGAAGS
     GSMKKMGSLG IKTIIWFEVI TTLVLGLGLL LANVLKPGVG LDLSHLAKKD IHELSGYTDK
     VVDFKQMILD IIPTNIIDVM ARNDLLAVIF FAILFGVAAA GIGKASEPVM KFFESTAQIM
     FKLTQIVMVT APIGVLALMA ASVGQYGIEL LLPMFKLVGT VFLGLFLILF VLFPLVGLIF
     QIKYFEVLKM IWDLFLIAFS TTSTETILPQ LMDRMEKYGC PKRVVSFVVP SGLSLNCDGS
     SLYLSVSCIF LAQAFQVDMT LSQQLLMMLV LVMTSKGIAA VPSGSLVVLL ATANAVGLPA
     EGVAIIAGVD RVMDMARTGV NVPGHAIACI VVSKWEKAFR QKEWVSANSQ TESI
//

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