ID   GADC_LACLA              Reviewed;         503 AA.
AC   Q9CG19; O50644;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Glutamate/gamma-aminobutyrate antiporter {ECO:0000250|UniProtKB:P63235};
DE            Short=Glu/GABA antiporter {ECO:0000250|UniProtKB:P63235};
GN   Name=gadC; OrderedLocusNames=LL1291; ORFNames=L125001;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 211-503.
RC   STRAIN=01-7;
RX   PubMed=10411264; DOI=10.1099/13500872-145-6-1375;
RA   Nomura M., Nakajima I., Fujita Y., Kobayashi M., Kimoto H., Suzuki I.,
RA   Aso H.;
RT   "Lactococcus lactis contains only one glutamate decarboxylase gene.";
RL   Microbiology 145:1375-1380(1999).
CC   -!- FUNCTION: Involved in glutaminase-dependent acid resistance. Exchanges
CC       extracellular glutamate (Glu) for intracellular gamma-aminobutyric acid
CC       (GABA) under acidic conditions. {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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {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; AE005176; AAK05389.1; -; Genomic_DNA.
DR   EMBL; AB010789; BAA24584.1; -; Genomic_DNA.
DR   PIR; C86786; C86786.
DR   RefSeq; NP_267447.1; NC_002662.1.
DR   RefSeq; WP_010905871.1; NC_002662.1.
DR   AlphaFoldDB; Q9CG19; -.
DR   SMR; Q9CG19; -.
DR   STRING; 272623.L125001; -.
DR   PaxDb; Q9CG19; -.
DR   EnsemblBacteria; AAK05389; AAK05389; L125001.
DR   KEGG; lla:L125001; -.
DR   PATRIC; fig|272623.7.peg.1394; -.
DR   eggNOG; COG0531; Bacteria.
DR   HOGENOM; CLU_020854_4_0_9; -.
DR   OMA; RIEPSRW; -.
DR   Proteomes; UP000002196; 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 membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..503
FT                   /note="Glutamate/gamma-aminobutyrate antiporter"
FT                   /id="PRO_0000213038"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        440..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         33..43
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        211..221
FT                   /note="EASASHINELE -> KLQLRTLMNLQ (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  55565 MW;  270FAE6EBEA533E8 CRC64;
     MNQKKISLFG FFALTASMVL TVYEYPTFAT SKLHLVFFLL LGGLLWFLPV ALCAAEMATV
     EGWKNGGIFS WVSQTLGERF GFAAIFFQWF QITVGFVTMI YFILGALSYV LNFQALNTDP
     LIKFIGLLII FWGLTFSQLG GTQRTAKLVK AGFVVGIVIP SIILFGLAAA YFIGGNPIEI
     PINKHAFVPD FSQVSTLVVF VSFILAYMGV EASASHINEL ENPKRNYPLA MILLVILAIS
     LDAIGGFSVA AVIPQKDLSL SAGVIQTFQT LILHFNHHLG WLVKVIALMI AFGVMGEVSS
     WVVGPSRGMF AAAQRGLLPK FLRKTNTHEV PVPLVMIQGI IVTLWGAVLT FGGGGNNLSF
     LVAISLTVVI YLVGYLLFFI GYFVLIYKKQ NLKRTYNVPG KRVGKTIIAG IGFLLSIFAL
     FISFVPPASI AKNETHTYQM ILLISFVVTA ILPFIVYELH DKRGHDTIEE PRHFKARDVN
     PAIYPAARGE HHIIKKEEHI LKH