GADC_SHIFL
ID GADC_SHIFL Reviewed; 511 AA.
AC P63236; P39183; P76131; P77384; Q54152;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 111.
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=SF1735, S1868;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M25-8A / Serotype 2a;
RX PubMed=8885264; DOI=10.1046/j.1365-2958.1996.00058.x;
RA Waterman S.R., Small P.L.C.;
RT "Identification of sigma S-dependent genes associated with the stationary-
RT phase acid-resistance phenotype of Shigella flexneri.";
RL Mol. Microbiol. 21:925-940(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
RN [4]
RP ACTIVITY REGULATION, AND INHIBITION BY L-PDC.
RC STRAIN=3136 / Serotype 2a;
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; U46133; AAD14843.1; -; Genomic_DNA.
DR EMBL; AE005674; AAN43310.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP17197.1; -; Genomic_DNA.
DR RefSeq; NP_707603.2; NC_004337.2.
DR RefSeq; WP_000246019.1; NZ_WPGW01000136.1.
DR AlphaFoldDB; P63236; -.
DR SMR; P63236; -.
DR STRING; 198214.SF1735; -.
DR EnsemblBacteria; AAN43310; AAN43310; SF1735.
DR EnsemblBacteria; AAP17197; AAP17197; S1868.
DR GeneID; 1024915; -.
DR GeneID; 66674656; -.
DR KEGG; sfl:SF1735; -.
DR KEGG; sfx:S1868; -.
DR PATRIC; fig|198214.7.peg.2055; -.
DR HOGENOM; CLU_020854_4_0_6; -.
DR OMA; RIEPSRW; -.
DR OrthoDB; 527053at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000213043"
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"
FT CONFLICT 212
FT /note="L -> G (in Ref. 1; AAD14843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 55077 MW; 85DF72B82816CE33 CRC64;
MATSVQTGKA 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
