ID   GATC_STAAT              Reviewed;         100 AA.
AC   A8Z2R5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C {ECO:0000255|HAMAP-Rule:MF_00122};
DE            Short=Asp/Glu-ADT subunit C {ECO:0000255|HAMAP-Rule:MF_00122};
DE            EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00122};
GN   Name=gatC {ECO:0000255|HAMAP-Rule:MF_00122};
GN   OrderedLocusNames=USA300HOU_1902;
OS   Staphylococcus aureus (strain USA300 / TCH1516).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=451516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300 / TCH1516;
RX   PubMed=17986343; DOI=10.1186/1471-2180-7-99;
RA   Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S.,
RA   Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O.,
RA   Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M.,
RA   Hemphill L., Ding Y., Dugan S., Blyth P.R., Buhay C.J., Dinh H.H.,
RA   Hawes A.C., Holder M., Kovar C.L., Lee S.L., Liu W., Nazareth L.V.,
RA   Wang Q., Zhou J., Kaplan S.L., Weinstock G.M.;
RT   "Subtle genetic changes enhance virulence of methicillin resistant and
RT   sensitive Staphylococcus aureus.";
RL   BMC Microbiol. 7:99-99(2007).
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; CP000730; ABX29904.1; -; Genomic_DNA.
DR   RefSeq; WP_000170162.1; NC_010079.1.
DR   AlphaFoldDB; A8Z2R5; -.
DR   SMR; A8Z2R5; -.
DR   GeneID; 66840130; -.
DR   KEGG; sax:USA300HOU_1902; -.
DR   HOGENOM; CLU_105899_1_2_9; -.
DR   OMA; VTPMAMK; -.
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..100
FT                   /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT                   subunit C"
FT                   /id="PRO_1000076199"
SQ   SEQUENCE   100 AA;  11268 MW;  7E9273A6AA979250 CRC64;
     MTKVTREEVE HIANLARLQI SPEETEEMAN TLESILDFAK QNDSADTEGV EPTYHVLDLQ
     NVLREDKAIK GIPQELALKN AKETEDGQFK VPTIMNEEDA