ID   GATC_BRUME              Reviewed;          95 AA.
AC   P64203; Q8YC58;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   01-MAY-2013, entry version 47.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C;
DE            Short=Glu-ADT subunit C;
DE            EC=6.3.5.-;
GN   Name=gatC; OrderedLocusNames=BMEII0674;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen
RT   Brucella melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn)
CC       or Gln-tRNA(Gln) through the transamidation of misacylated Asp-
CC       tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both
CC       of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC       + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP
CC       + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits (By similarity).
CC   -!- SIMILARITY: Belongs to the GatC family.
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DR   EMBL; AE008918; AAL53916.1; -; Genomic_DNA.
DR   PIR; AI3593; AI3593.
DR   RefSeq; NP_541652.1; NC_003318.1.
DR   ProteinModelPortal; P64203; -.
DR   STRING; 224914.BMEII0674; -.
DR   PRIDE; P64203; -.
DR   EnsemblBacteria; AAL53916; AAL53916; BMEII0674.
DR   GeneID; 1198446; -.
DR   KEGG; bme:BMEII0674; -.
DR   PATRIC; 17799730; VBIBruMel146950_2201.
DR   HOGENOM; HOG000017522; -.
DR   KO; K02435; -.
DR   OMA; SVTPMAM; -.
DR   ProtClustDB; PRK00034; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR   GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:HAMAP.
DR   HAMAP; MF_00122; GatC; 1; -.
DR   InterPro; IPR003837; Asp/Glu-ADT_csu.
DR   Pfam; PF02686; Glu-tRNAGln; 1.
DR   TIGRFAMs; TIGR00135; gatC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1     95       Glutamyl-tRNA(Gln) amidotransferase
FT                                subunit C.
FT                                /FTId=PRO_0000105283.
SQ   SEQUENCE   95 AA;  10303 MW;  AFCEDB571ACAB124 CRC64;
     MSVDISTVKR VAHLARIAVS EDDAERMTGE LNAILGFVEQ LNEVDVEGIE PMTSVTPMKM
     RMREDKVTDG GIAAAVVANA PVTEDNFFVV PKVVE
//

ID   D0B731_BRUME            Unreviewed;        95 AA.
AC   D0B731;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   03-APR-2013, entry version 26.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C;
DE            Short=Asp/Glu-ADT subunit C;
DE            EC=6.3.5.-;
GN   Name=gatC; ORFNames=BAWG_1902;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=16M;
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T.,
RA   Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M.,
RA   Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.;
RT   "The Genome Sequence of Brucella melitensis bv. 1 str. 16M.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn)
CC       or Gln-tRNA(Gln) through the transamidation of misacylated Asp-
CC       tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both
CC       of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP
CC       + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC       + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits (By similarity).
CC   -!- SIMILARITY: Belongs to the GatC family.
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DR   EMBL; GG703779; EEW87423.1; -; Genomic_DNA.
DR   RefSeq; NP_541652.1; NC_003318.1.
DR   ProteinModelPortal; D0B731; -.
DR   STRING; D0B731; -.
DR   PRIDE; D0B731; -.
DR   EnsemblBacteria; EEW87423; EEW87423; BAWG_1902.
DR   GeneID; 1198446; -.
DR   KEGG; bme:BMEII0674; -.
DR   PATRIC; 17799730; VBIBruMel146950_2201.
DR   eggNOG; COG0721; -.
DR   KO; K02435; -.
DR   OMA; SVTPMAM; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:HAMAP.
DR   HAMAP; MF_00122; GatC; 1; -.
DR   InterPro; IPR003837; Asp/Glu-ADT_csu.
DR   Pfam; PF02686; Glu-tRNAGln; 1.
DR   TIGRFAMs; TIGR00135; gatC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis;
KW   Transferase.
SQ   SEQUENCE   95 AA;  10303 MW;  AFCEDB571ACAB124 CRC64;
     MSVDISTVKR VAHLARIAVS EDDAERMTGE LNAILGFVEQ LNEVDVEGIE PMTSVTPMKM
     RMREDKVTDG GIAAAVVANA PVTEDNFFVV PKVVE
//