ID   GATA_CHLMU              Reviewed;         491 AA.
AC   Q9PL37;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE            Short=Glu-ADT subunit A;
DE            EC=6.3.5.7;
GN   Name=gatA; OrderedLocusNames=TC_0271;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in organisms
CC       which lack glutaminyl-tRNA synthetase. The reaction takes place in the
CC       presence of glutamine and ATP through an activated gamma-phospho-Glu-
CC       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; EC=6.3.5.7;
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE002160; AAF39139.1; -; Genomic_DNA.
DR   PIR; A81722; A81722.
DR   RefSeq; WP_010229994.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PL37; -.
DR   SMR; Q9PL37; -.
DR   STRING; 243161.TC_0271; -.
DR   EnsemblBacteria; AAF39139; AAF39139; TC_0271.
DR   GeneID; 1246441; -.
DR   KEGG; cmu:TC_0271; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_0; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1239251at2; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:InterPro.
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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   HAMAP; MF_00120; GatA; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR004412; GatA.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   TIGRFAMs; TIGR00132; gatA; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..491
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105150"
FT   ACT_SITE        77
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        152
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        176
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   491 AA;  53543 MW;  5806B0302B158458 CRC64;
     MYRKSALELR DAVVNREISV TAITEYFYHR IESYDEQIGS FLSLCKERAL LRASRIDDKL
     AKGDPIGILA GIPIGVKDNI HITGVKTTCA SKMLENFVAP FDATVVRRIE MEDGILLGKL
     NMDEFAMGST TRYSAFQHTN NPWDLERVPG GSSGGSAAAV SARFCPIALG SDTGGSIRQP
     AAFCGVVGFK PSYGAVSRYG LVAFGSSLDQ IGPLTTVVED VALAMDAFAG RDIKDATTRD
     FFRGTFSQAL SLEVPKLIGV PRGFLDGLQE DCKENFFEAL AVMERQGSRI IDIDLSVLKH
     AVPVYYIVAS AEAATNLARF DGVRYGHRCA QADNMQEMYA RSRKEGFGKE VTRRILLGNY
     VLSAERQNIF YKKGTAVRAT LIEAFQSAFE CCDVIAMPVC ASPAIRDTDV LDPVSLYLQD
     IYTVAVNLAY LPAISVPSGL SKEGLPLGVQ FIGKRGADQQ ICQVGYSFQE HSQIKQLYPK
     AVNGLFDGGM E