ID   GATC_GEOSE              Reviewed;          96 AA.
AC   P58250;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C;
DE            Short=Glu-ADT subunit C;
DE            EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00122};
GN   Name=gatC {ECO:0000255|HAMAP-Rule:MF_00122};
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kwak J.H., Shin K., Kim S.I.;
RT   "Glu-tRNAGln amidotransferase of Bacillus stearothermophilus.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or
CC       Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn)
CC       or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-
CC       tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the
CC       presence of glutamine and ATP through an activated phospho-Asp-
CC       tRNA(Asn) or phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_00122}.
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;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00122};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+)
CC         + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00122};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00122}.
CC   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00122}.
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DR   EMBL; AY040860; AAK72611.1; -; Genomic_DNA.
DR   AlphaFoldDB; P58250; -.
DR   SMR; P58250; -.
DR   GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
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:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00122; GatC; 1.
DR   InterPro; IPR003837; Asp/Glu-ADT_csu.
DR   InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR   PANTHER; PTHR15004; PTHR15004; 1.
DR   Pfam; PF02686; Glu-tRNAGln; 1.
DR   SUPFAM; SSF141000; SSF141000; 1.
DR   TIGRFAMs; TIGR00135; gatC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..96
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit C"
FT                   /id="PRO_0000105275"
SQ   SEQUENCE   96 AA;  10909 MW;  D7D98FF79EB6F5BB CRC64;
     MSRISIEQVK HVADLARLAI TDEEAEMFTK QLDAIITFAE QLNELDTENV PPTSHVLDMR
     NVMREDIPEP GLPREEVLKN APDQQDGQFR VPAILE