GATA_STRP1
ID GATA_STRP1 Reviewed; 488 AA.
AC Q99YC0; Q48X00;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 127.
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};
GN OrderedLocusNames=SPy_1771, M5005_Spy1507;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
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 -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00120}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004092; AAK34510.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ52125.1; -; Genomic_DNA.
DR RefSeq; NP_269789.1; NC_002737.2.
DR AlphaFoldDB; Q99YC0; -.
DR SMR; Q99YC0; -.
DR STRING; 1314.HKU360_01561; -.
DR PaxDb; Q99YC0; -.
DR EnsemblBacteria; AAK34510; AAK34510; SPy_1771.
DR KEGG; spy:SPy_1771; -.
DR KEGG; spz:M5005_Spy1507; -.
DR PATRIC; fig|160490.10.peg.1540; -.
DR HOGENOM; CLU_009600_0_3_9; -.
DR OMA; EVSCPHF; -.
DR Proteomes; UP000000750; 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;
KW Reference proteome.
FT CHAIN 1..488
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000105213"
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"
FT CONFLICT 185
FT /note="S -> G (in Ref. 2; AAZ52125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 52320 MW; F669D53140358EFD CRC64;
MSFNHKTIEE LHDLLVAKEI SATELTQATL EDIKSREEAV GSFITVSEEV ALKQAAAIDA
KGIDADNLMS GIPLAVKDNI STKEILTTAA SKMLYNYEPI FNATSVANAY AKDMIVIGKT
NMDEFAMGGS TETSYFKKTK NAWDHTKVPG GSSGGSATAV ASGQVRLSLG SDTGGSIRQP
AAFNSVVGLK PTYGTVSRYG LIAFGSSLDQ IGPFAPTVKE NAQLLNVIAS SDVKDATSAP
VRIADYTSKI GRDIKGMKIA LPKEYLGEGI DPEIKETVLA SVKQFEALGA TVEEVSLPHS
KYGVAVYYII ASSEASSNLQ RFDGIRYGFR ADDAKNLDEI YVNTRSQGFG DEVKRRIMLG
TFSLSSGYYD AYFKKAGQVR TLIIQDFDKV FADYDLILGP TTPTVAFGLD TLNHDPVAMY
LADLLTIPVN LAGLPGISIP AGFVDGLPVG LQLIGPKYAE ETIYQAAAAF EAVTDYHKQQ
PIIFGGDK
