ID   GATC_BACSU              Reviewed;          96 AA.
AC   O06492;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C;
DE            Short=Glu-ADT subunit C;
DE            EC=6.3.5.-;
GN   Name=gatC; Synonyms=yedA, yerL; OrderedLocusNames=BSU06670;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9342321; DOI=10.1073/pnas.94.22.11819;
RA   Curnow A.W., Hong K.-W., Yuan R., Kim S.-I., Martins O., Winkler W.,
RA   Henkin T.M., Soell D.;
RT   "Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for
RT   correct decoding of glutamine codons during translation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:11819-11826(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969499; DOI=10.1099/13500872-142-11-3027;
RA   Borriss R., Porwollik S., Schroeter R.;
RT   "The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a
RT   region devoted to purine uptake and metabolism, and containing the genes
RT   cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide
RT   sequence.";
RL   Microbiology 142:3027-3031(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=11902719; DOI=10.1046/j.1365-2958.1997.4441809.x;
RA   von Blohn C., Kempf B., Kappes R.M., Bremer E.;
RT   "Osmostress response in Bacillus subtilis: characterization of a proline
RT   uptake system (OpuE) regulated by high osmolarity and the alternative
RT   transcription factor sigma B.";
RL   Mol. Microbiol. 25:175-187(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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) (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;
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   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB72183.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF008553; AAB83963.1; -; Genomic_DNA.
DR   EMBL; AF011545; AAB72183.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U92466; AAB66514.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12487.1; -; Genomic_DNA.
DR   PIR; T44451; T44451.
DR   RefSeq; NP_388549.1; NC_000964.3.
DR   RefSeq; WP_003219442.1; NZ_JNCM01000032.1.
DR   AlphaFoldDB; O06492; -.
DR   SMR; O06492; -.
DR   STRING; 224308.BSU06670; -.
DR   jPOST; O06492; -.
DR   PaxDb; O06492; -.
DR   PRIDE; O06492; -.
DR   EnsemblBacteria; CAB12487; CAB12487; BSU_06670.
DR   GeneID; 64302530; -.
DR   GeneID; 936063; -.
DR   KEGG; bsu:BSU06670; -.
DR   PATRIC; fig|224308.179.peg.725; -.
DR   eggNOG; COG0721; Bacteria.
DR   InParanoid; O06492; -.
DR   OMA; VTPMAMK; -.
DR   PhylomeDB; O06492; -.
DR   BioCyc; BSUB:BSU06670-MON; -.
DR   BioCyc; MetaCyc:MON-13957; -.
DR   PRO; PR:O06492; -.
DR   Proteomes; UP000001570; Chromosome.
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; IBA:GO_Central.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..96
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit C"
FT                   /id="PRO_0000105276"
SQ   SEQUENCE   96 AA;  10859 MW;  78B586BC3F62A8FF CRC64;
     MSRISIEEVK HVAHLARLAI TEEEAKMFTE QLDSIISFAE ELNEVNTDNV EPTTHVLKMK
     NVMREDEAGK GLPVEDVMKN APDHKDGYIR VPSILD