ID   GATA_STRPN              Reviewed;         488 AA.
AC   Q97SE6;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            Short=Glu-ADT subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_00120};
GN   Name=gatA {ECO:0000255|HAMAP-Rule:MF_00120}; OrderedLocusNames=SP_0437;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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). {ECO:0000255|HAMAP-Rule:MF_00120}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00120};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00120}.
CC   -!- INTERACTION:
CC       Q97SE6; Q97QS2: eno; NbExp=2; IntAct=EBI-2207039, EBI-2207206;
CC       Q97SE6; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207039, EBI-2207053;
CC       Q97SE6; Q97NV3: groES; NbExp=2; IntAct=EBI-2207039, EBI-2206949;
CC       Q97SE6; P0CB75: pyrF; NbExp=2; IntAct=EBI-2207039, EBI-2207109;
CC       Q97SE6; Q97NX5: scpA; NbExp=2; IntAct=EBI-2207039, EBI-2207368;
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00120}.
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DR   EMBL; AE005672; AAK74599.1; -; Genomic_DNA.
DR   PIR; F95050; F95050.
DR   RefSeq; WP_000143747.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q97SE6; -.
DR   SMR; Q97SE6; -.
DR   IntAct; Q97SE6; 5.
DR   STRING; 170187.SP_0437; -.
DR   EnsemblBacteria; AAK74599; AAK74599; SP_0437.
DR   KEGG; spn:SP_0437; -.
DR   eggNOG; COG0154; Bacteria.
DR   OMA; EVSCPHF; -.
DR   PhylomeDB; Q97SE6; -.
DR   BioCyc; SPNE170187:G1FZB-452-MON; -.
DR   Proteomes; UP000000585; 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   1: Evidence at protein level;
KW   ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..488
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105212"
FT   ACT_SITE        77
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        152
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        176
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   488 AA;  52060 MW;  9D54C56883F62C91 CRC64;
     MTFNNKTIEE LHNLLVSKEI SATELTQATL ENIKSREEAL NSFVTIAEEQ ALVQAKAIDE
     AGIDADNVLS GIPLAVKDNI STDGILTTAA SKMLYNYEPI FDATAVANAK TKGMIVVGKT
     NMDEFAMGGS GETSHYGATK NAWNHSKVPG GSSSGSAAAV ASGQVRLSLG SDTGGSIRQP
     AAFNGIVGLK PTYGTVSRFG LIAFGSSLDQ IGPFAPTVKE NALLLNAIAS EDAKDSTSAP
     VRIADFTSKI GQDIKGMKIA LPKEYLGEGI DPEVKETILN AAKHFEKLGA IVEEVSLPHS
     KYGVAVYYII ASSEASSNLQ RFDGIRYGYR AEDATNLDEI YVNSRSQGFG EEVKRRIMLG
     TFSLSSGYYD AYYKKAGQVR TLIIQDFEKV FADYDLILGP TAPSVAYDLD SLNHDPVAMY
     LADLLTIPVN LAGLPGISIP AGFSQGLPVG LQLIGPKYSE ETIYQAAAAF EATTDYHKQQ
     PVIFGGDN