ID   GADC_LACLM              Reviewed;         503 AA.
AC   O30417; A2RKG1;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Glutamate/gamma-aminobutyrate antiporter {ECO:0000303|PubMed:9484886};
DE            Short=Glu/GABA antiporter {ECO:0000250|UniProtKB:P63235};
GN   Name=gadC {ECO:0000303|PubMed:9484886}; OrderedLocusNames=llmg_1178;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX   PubMed=9484886; DOI=10.1046/j.1365-2958.1998.00676.x;
RA   Sanders J.W., Leenhouts K., Burghoorn J., Brands J.R., Venema G., Kok J.;
RT   "A chloride-inducible acid resistance mechanism in Lactococcus lactis and
RT   its regulation.";
RL   Mol. Microbiol. 27:299-310(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-119.
RX   PubMed=9604892; DOI=10.1007/s004380050697;
RA   Sanders J.W., Venema G., Kok J., Leenhouts K.;
RT   "Identification of a sodium chloride-regulated promoter in Lactococcus
RT   lactis by single-copy chromosomal fusion with a reporter gene.";
RL   Mol. Gen. Genet. 257:681-685(1998).
CC   -!- FUNCTION: Involved in glutaminase-dependent acid resistance
CC       (PubMed:9484886). Exchanges extracellular glutamate (Glu) for
CC       intracellular gamma-aminobutyric acid (GABA) under acidic conditions
CC       (By similarity). {ECO:0000250|UniProtKB:P63235,
CC       ECO:0000269|PubMed:9484886}.
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:0000250|UniProtKB:P63235};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P63235}.
CC   -!- INDUCTION: Expression is highest at onset of stationary phase in
CC       presence of NaCl and glutamate, and at low pH. Chloride-dependent
CC       expression is activated by GadR. {ECO:0000269|PubMed:9484886}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAL97771.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF005098; AAC46187.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97771.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_014735013.1; NZ_WJVF01000010.1.
DR   AlphaFoldDB; O30417; -.
DR   SMR; O30417; -.
DR   STRING; 416870.llmg_1178; -.
DR   TCDB; 2.A.3.7.1; the amino acid-polyamine-organocation (apc) family.
DR   EnsemblBacteria; CAL97771; CAL97771; llmg_1178.
DR   KEGG; llm:llmg_1178; -.
DR   eggNOG; COG0531; Bacteria.
DR   HOGENOM; CLU_020854_4_0_9; -.
DR   OMA; RIEPSRW; -.
DR   BioCyc; LLAC416870:LLMG_RS05965-MON; -.
DR   Proteomes; UP000000364; 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   2: Evidence at transcript level;
KW   Amino-acid transport; Antiport; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..503
FT                   /note="Glutamate/gamma-aminobutyrate antiporter"
FT                   /id="PRO_0000213039"
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"
SQ   SEQUENCE   503 AA;  55369 MW;  9AD30F9FCE699846 CRC64;
     MNQKKLSLFG FFALTASMVL TVYEYPTFAT SKLHLVFFLL LGGLLWFLPV ALCAAEMATV
     EGWKNGGIFS WVSQTLGERF GFAAIFFQWF QITVGFVTMI YFILGALSYV LNFQALNTDP
     LIKFIGLLII FWGLTFSQLG GTQRTAKLVK AGFVVGIVIP SVILFGLAAA YFIGGNPIEI
     PINSHAFVPD FSQVSTLVVF VSFILAYMGV EASASHINEL ENPKRNYPLA MILLVILAIS
     LDAIGGFSVA AVIPQKELSL SAGVIQTFQT LILHFNHHLG WLVKVIALMI AFGVMGEVSS
     WVVGPSRGMF AAAQRGLLPK FLRKTNTHEV PVPLVMIQGI IVTLWGAVLT FGGGGNNLSF
     LVAISLTVVI YLVGYLLFFI VYFVLIYKKQ NLKRTYNVPG KIIGKTIIAG IGFLLSIFAL
     FISFVPPASI AKNETHTYQM ILLISFVVTA ILPFIIYELH DKKGHDTIEE PTHFKAGDVN
     PAIYPAARGE HHIIKKEEHI LKH