ID   GATC_OPITP              Reviewed;          94 AA.
AC   B1ZQN2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   19-OCT-2011, entry version 29.
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; OrderedLocusNames=Oter_2359;
OS   Opitutus terrae (strain DSM 11246 / PB90-1).
OC   Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae;
OC   Opitutus.
OX   NCBI_TaxID=452637;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11246 / PB90-1;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Pitluck S.,
RA   Goltsman E., Clum A., Sun H., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Smidt H., Richardson P.;
RT   "Complete sequence of Opitutus terrae PB90-1.";
RL   Submitted (APR-2008) 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-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; CP001032; ACB75641.1; -; Genomic_DNA.
DR   RefSeq; YP_001819241.1; NC_010571.1.
DR   ProteinModelPortal; B1ZQN2; -.
DR   STRING; B1ZQN2; -.
DR   GeneID; 6206477; -.
DR   GenomeReviews; CP001032_GR; Oter_2359.
DR   KEGG; ote:Oter_2359; -.
DR   HOGENOM; HBG586403; -.
DR   OMA; NIWREDE; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   HAMAP; MF_00122; GatC; 1; -.
DR   InterPro; IPR003837; Glu-tRNAGlntrans.
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     94       Aspartyl/glutamyl-tRNA(Asn/Gln)
FT                                amidotransferase subunit C.
FT                                /FTId=PRO_1000122578.
SQ   SEQUENCE   94 AA;  10051 MW;  5E9479420C801673 CRC64;
     MATDLNIDHV ANLARLALTP EEKATFAQQL GDVLHHIEQL AKVDVAGVEP TAHAFAVTNV
     WADDAPQPGL SVEAALKNAP AQREHMVVVP KVVE
//