ID   GATC_CHLTR              Reviewed;         100 AA.
AC   O84005;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   02-SEP-2026, entry version 112.
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};
GN   Name=gatC {ECO:0000255|HAMAP-Rule:MF_00122}; OrderedLocusNames=CT_002;
OS   Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx).
OC   Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
OC   Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-885 / DSM 19411 / UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- FUNCTION: Structural subunit of the Asp/Glu-tRNA(Asn/Gln)
CC       amidotransferase complex GatCAB. GatCAB allows the formation of
CC       correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the multi-step
CC       transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in
CC       organisms which lack either or both of asparaginyl-tRNA or glutaminyl-
CC       tRNA synthetases. The reaction takes place in the presence of glutamine
CC       and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-
CC       tRNA(Gln). This subunit forms a belt that wraps around the interface of
CC       the catalytic subunits A and B to stabilize the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00122}.
CC   -!- SUBUNIT: Component of the heterotrimeric GatCAB glutamyl-tRNA(Gln)
CC       amidotransferase complex composed of GatA, GatB and GatC.
CC       {ECO:0000255|HAMAP-Rule:MF_00122}.
CC   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00122, ECO:0000305}.
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DR   EMBL; AE001273; AAC67592.1; -; Genomic_DNA.
DR   PIR; E71568; E71568.
DR   RefSeq; NP_219504.1; NC_000117.1.
DR   RefSeq; WP_009871348.1; NC_000117.1.
DR   AlphaFoldDB; O84005; -.
DR   SMR; O84005; -.
DR   STRING; 272561.CT_002; -.
DR   EnsemblBacteria; AAC67592; AAC67592; CT_002.
DR   GeneID; 884067; -.
DR   KEGG; ctr:CT_002; -.
DR   PATRIC; fig|272561.5.peg.3; -.
DR   HOGENOM; CLU_105899_1_2_0; -.
DR   InParanoid; O84005; -.
DR   OrthoDB; 18187at2; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
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; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR   InterPro; IPR003837; GatC.
DR   NCBIfam; TIGR00135; gatC; 1.
DR   Pfam; PF02686; GatC; 1.
DR   SUPFAM; SSF141000; Glu-tRNAGln amidotransferase C subunit; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..100
FT                   /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT                   subunit C"
FT                   /id="PRO_0000105291"
SQ   SEQUENCE   100 AA;  11074 MW;  16264B181F8771AC CRC64;
     MTESYVNKEE IISLAKNAAL ELEDAHVEEF VTSMNDVIAL MQEVIAIDIS DIILEATVHH
     FVGPEDLRED MVTSDFTQEE FLSNVPVSLG GLVKVPTVIK
//