ID   GATA_LIGS1              Reviewed;         487 AA.
AC   Q1WSH9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            Short=Glu-ADT subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_00120};
GN   Name=gatA {ECO:0000255|HAMAP-Rule:MF_00120}; OrderedLocusNames=LSL_1345;
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118;
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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). {ECO:0000255|HAMAP-Rule:MF_00120}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00120};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00120}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00120}.
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DR   EMBL; CP000233; ABE00150.1; -; Genomic_DNA.
DR   RefSeq; WP_011476296.1; NC_007929.1.
DR   RefSeq; YP_536233.1; NC_007929.1.
DR   AlphaFoldDB; Q1WSH9; -.
DR   SMR; Q1WSH9; -.
DR   STRING; 362948.LSL_1345; -.
DR   EnsemblBacteria; ABE00150; ABE00150; LSL_1345.
DR   KEGG; lsl:LSL_1345; -.
DR   PATRIC; fig|362948.14.peg.1420; -.
DR   HOGENOM; CLU_009600_0_3_9; -.
DR   OMA; EVSCPHF; -.
DR   Proteomes; UP000006559; 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..487
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_1000015850"
FT   ACT_SITE        77
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        152
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        176
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   487 AA;  52778 MW;  F437B133A6BAE302 CRC64;
     MDYFKNDLAS IHDDLVNKKY SVEELTKSTF DNIKKVDKEI EAFLKLDEER ALEKARKIDE
     RGVKADSILD GIGIGIKDNI VTKDLTTTAA SKMLENFEPI YNATVMDKLN DAGMITVGKL
     NMDEFAMGSS TENSAFKITK NVWDTTKVPG GSSGGSAAAV ASGQVLASLG SDTGGSIRQP
     AAFNGIVGVK PTYGRVSRYG LIAFASSLDQ IGPLTRTVKD NALVLNAISG HDAHDFTSSS
     REVPDFTKGI EDGVKGMRIA VPKEYFGEGV DEDVAKAVKD AVKTFESLGA TVDEISLPHS
     KYGVPVYYII ASSEASSNLQ RYDGIRYGFR AKDVKNLEDV YVRSRSEGFG DEVKRRIMLG
     TFSLSAGSYD AFFKKAAQVR TLICQDFENV YKDYDLILAP TSPTTAYGIG EEINDPVTMY
     MNDILTIPVN LAGLPGMSLP AGFSNGLPIG LQLIAPRFAE STMYRAGYAF EQSTDFHKAI
     PTLGGQN