ID   GATA_CAMJE              Reviewed;         453 AA.
AC   Q9PNN2; Q0P9J3;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE            Short=Glu-ADT subunit A;
DE            EC=6.3.5.7;
GN   Name=gatA; OrderedLocusNames=Cj1059c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in organisms
CC       which lack glutaminyl-tRNA synthetase. The reaction takes place in the
CC       presence of glutamine and ATP through an activated gamma-phospho-Glu-
CC       tRNA(Gln) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC         L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC         Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; EC=6.3.5.7;
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL111168; CAL35177.1; -; Genomic_DNA.
DR   PIR; H81308; H81308.
DR   RefSeq; WP_002853884.1; NC_002163.1.
DR   RefSeq; YP_002344454.1; NC_002163.1.
DR   AlphaFoldDB; Q9PNN2; -.
DR   SMR; Q9PNN2; -.
DR   IntAct; Q9PNN2; 5.
DR   STRING; 192222.Cj1059c; -.
DR   PaxDb; Q9PNN2; -.
DR   PRIDE; Q9PNN2; -.
DR   EnsemblBacteria; CAL35177; CAL35177; Cj1059c.
DR   GeneID; 905351; -.
DR   KEGG; cje:Cj1059c; -.
DR   PATRIC; fig|192222.6.peg.1041; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_7; -.
DR   OMA; EVSCPHF; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   HAMAP; MF_00120; GatA; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR004412; GatA.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   TIGRFAMs; TIGR00132; gatA; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..453
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105147"
FT   ACT_SITE        56
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        131
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        155
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   453 AA;  49284 MW;  6A6764163B417633 CRC64;
     MITLKEALKY SKEELENLKK ELNEKAKKEK KLGAYIEQFL DKDLSVSGEG VPVAIKDNIS
     VKGWELTSAS KILQGYIAPY DASAIVNLKA NGFSPFGRCN MDEFAMGSST ASSCYGKTLN
     PLNFERVPGG SSGGSAAAVA GGLALASLGS DTGGSVRQPA AFCGCVGFKP SYGRVSRYGL
     ASYSSSLDQI GVLTQNVEDA AILYDAIAGY DKMDSTSANI EFIKTVPNLN ANKKLKIAVI
     ENYVNDADSE VKNALLKTID MLKANGHEIV YKNLLDSKFD IAAYYIIATA EASANLSRYD
     GVRYGKRSEN IQNLKEMYVN TRSEGFGEEV KRRILLGTFV LSSGYYDAYY IKAQKARAFI
     KAKYEEILQD CDLIFMPVTP TTAFKFDTQK SPMQTYLEDV YTISVNLAGL GGISVPVAKD
     KEGLNISAQL ICKAYDEQTL LDGALSLEQM IKN