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GADC_ECO57
ID   GADC_ECO57              Reviewed;         511 AA.
AC   P58229;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Glutamate/gamma-aminobutyrate antiporter {ECO:0000250|UniProtKB:P63235};
DE            Short=Glu/GABA antiporter {ECO:0000250|UniProtKB:P63235};
GN   Name=gadC; Synonyms=acsA, xasA; OrderedLocusNames=Z2216, ECs2097;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   ACTIVITY REGULATION, AND INHIBITION BY L-PDC.
RX   PubMed=12855178; DOI=10.1016/s0378-1097(03)00427-0;
RA   Waterman S.R., Small P.L.C.;
RT   "The glutamate-dependent acid resistance system of Escherichia coli and
RT   Shigella flexneri is inhibited in vitro by L-trans-pyrrolidine-2,4-
RT   dicarboxylic acid.";
RL   FEMS Microbiol. Lett. 224:119-125(2003).
CC   -!- FUNCTION: Involved in glutaminase-dependent acid resistance. Exchanges
CC       extracellular glutamate (Glu) for intracellular gamma-aminobutyric acid
CC       (GABA) under acidic conditions. The ability to survive the extremely
CC       acidic conditions of the stomach is essential for successful
CC       colonization of the host by commensal and pathogenic bacteria.
CC       {ECO:0000250|UniProtKB:P63235}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-aminobutanoate(in) + L-glutamate(out) = 4-
CC         aminobutanoate(out) + L-glutamate(in); Xref=Rhea:RHEA:28919,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888;
CC         Evidence={ECO:0000250|UniProtKB:P63235};
CC   -!- ACTIVITY REGULATION: Shows pH-dependent activity (By similarity). The
CC       glutamate analog L-trans-pyrrolidine-2,4-dicarboxylic acid (L-PDC)
CC       blocks the uptake of glutamate by selective inhibition
CC       (PubMed:12855178). {ECO:0000250|UniProtKB:P63235,
CC       ECO:0000269|PubMed:12855178}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P63235}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P63235}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. Glutamate:GABA antiporter (GGA) (TC 2.A.3.7) family.
CC       {ECO:0000305}.
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DR   EMBL; AE005174; AAG56276.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35520.1; -; Genomic_DNA.
DR   PIR; A90891; A90891.
DR   PIR; H85726; H85726.
DR   RefSeq; NP_310124.1; NC_002695.1.
DR   RefSeq; WP_000224402.1; NZ_SEKU01000015.1.
DR   AlphaFoldDB; P58229; -.
DR   SMR; P58229; -.
DR   STRING; 155864.EDL933_2148; -.
DR   EnsemblBacteria; AAG56276; AAG56276; Z2216.
DR   EnsemblBacteria; BAB35520; BAB35520; ECs_2097.
DR   GeneID; 917297; -.
DR   KEGG; ece:Z2216; -.
DR   KEGG; ecs:ECs_2097; -.
DR   PATRIC; fig|386585.9.peg.2202; -.
DR   eggNOG; COG0531; Bacteria.
DR   HOGENOM; CLU_020854_4_0_6; -.
DR   OMA; RIEPSRW; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004759; Glu_antiport.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   TIGRFAMs; TIGR00910; 2A0307_GadC; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Antiport; Cell inner membrane; Cell membrane;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport; Virulence.
FT   CHAIN           1..511
FT                   /note="Glutamate/gamma-aminobutyrate antiporter"
FT                   /id="PRO_0000213042"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..41
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        63..93
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..127
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..200
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..239
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..291
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..335
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        357..366
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        388..412
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        434..445
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        446..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        467..511
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   511 AA;  55103 MW;  85DF72BD2529CE33 CRC64;
     MATLVQTGKA KQLTLLGFFA ITASMVMAVY EYPTFATSGF SLVFFLLLGG ILWFIPVGLC
     AAEMATVDGW EEGGVFAWVS NTLGPRWGFA AISFGYLQIA IGFIPMLYFV LGALSYILKW
     PALNEDPITK TIAALIILWA LALTQFGGTK YTARIAKVGF FAGILLPAFI LIALAAIYLH
     SGAPVAIEMD SKTFFPDFSK VGTLVVFVAF ILSYMGVEAS ATHVNEMSNP GRDYPLAMLL
     LMVAAICLSS VGGLSIAMVI PGNEINLSAG VMQTFTVLMS HVAPEIEWTV RVISALLLLG
     VLAEIASWIV GPSRGMYVTA QKNLLPAAFA KMNKNGVPVT LVISQLVITS IALIILTNTG
     GGNNMSFLIA LALTVVIYLC AYFMLFIGYI VLVLKHPDLK RTFNIPGGKG VKLVVAIVGL
     LTSIMAFIVS FLPPDNIQGD STDMYVELLV VSFLVVLALP FILYAVHDRK GKANTGVTLE
     PINSQNAPKG HFFLHPRARS PHYIVMNDKK H
 
 
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