GATC_STRPN
ID GATC_STRPN Reviewed; 100 AA.
AC Q97SE5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C;
DE Short=Glu-ADT subunit C;
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00122};
GN Name=gatC {ECO:0000255|HAMAP-Rule:MF_00122}; OrderedLocusNames=SP_0438;
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 Asn-tRNA(Asn) or
CC Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn)
CC or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-
CC tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the
CC presence of glutamine and ATP through an activated phospho-Asp-
CC tRNA(Asn) or phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_00122}.
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+)
CC + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00122};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_00122}.
CC -!- INTERACTION:
CC Q97SE5; P0A2W6: acpS; NbExp=2; IntAct=EBI-2207053, EBI-2207344;
CC Q97SE5; Q97SU1: adk; NbExp=2; IntAct=EBI-2207053, EBI-2206969;
CC Q97SE5; P63544: apt; NbExp=2; IntAct=EBI-2207053, EBI-2207316;
CC Q97SE5; Q54869: argS; NbExp=2; IntAct=EBI-2207053, EBI-2207421;
CC Q97SE5; Q9S400: aroA; NbExp=2; IntAct=EBI-2207053, EBI-2207276;
CC Q97SE5; P63588: aroD; NbExp=2; IntAct=EBI-2207053, EBI-2207290;
CC Q97SE5; Q97PR0: asnS; NbExp=2; IntAct=EBI-2207053, EBI-2207302;
CC Q97SE5; Q97R25: dapA; NbExp=2; IntAct=EBI-2207053, EBI-2207165;
CC Q97SE5; P95830: dnaJ; NbExp=2; IntAct=EBI-2207053, EBI-2207079;
CC Q97SE5; Q97QS2: eno; NbExp=2; IntAct=EBI-2207053, EBI-2207206;
CC Q97SE5; Q97SE6: gatA; NbExp=2; IntAct=EBI-2207053, EBI-2207039;
CC Q97SE5; Q97SE7: gatB; NbExp=3; IntAct=EBI-2207053, EBI-2207023;
CC Q97SE5; Q97NV3: groES; NbExp=2; IntAct=EBI-2207053, EBI-2206949;
CC Q97SE5; Q97S73: grpE; NbExp=2; IntAct=EBI-2207053, EBI-2207065;
CC Q97SE5; P65144: infC; NbExp=2; IntAct=EBI-2207053, EBI-2207149;
CC Q97SE5; A0A0H2UNP1: lacF-1; NbExp=2; IntAct=EBI-2207053, EBI-2207447;
CC Q97SE5; Q97RS9: lysS; NbExp=2; IntAct=EBI-2207053, EBI-2207121;
CC Q97SE5; P0A4T1: malR; NbExp=2; IntAct=EBI-2207053, EBI-2207435;
CC Q97SE5; Q97Q68: mecA; NbExp=2; IntAct=EBI-2207053, EBI-2207260;
CC Q97SE5; P41354: mutX; NbExp=2; IntAct=EBI-2207053, EBI-2207232;
CC Q97SE5; P0CB78: pyrE; NbExp=2; IntAct=EBI-2207053, EBI-2207897;
CC Q97SE5; P0CB75: pyrF; NbExp=2; IntAct=EBI-2207053, EBI-2207109;
CC Q97SE5; P65946: pyrR; NbExp=2; IntAct=EBI-2207053, EBI-2207248;
CC Q97SE5; Q97QV8: rex; NbExp=2; IntAct=EBI-2207053, EBI-2207177;
CC Q97SE5; Q97NX6: scpB; NbExp=2; IntAct=EBI-2207053, EBI-2206697;
CC Q97SE5; P0A4J6: sodA; NbExp=2; IntAct=EBI-2207053, EBI-2207137;
CC Q97SE5; A0A0H2UPY3: SP_1103; NbExp=2; IntAct=EBI-2207053, EBI-2207193;
CC Q97SE5; P67049: thyA; NbExp=2; IntAct=EBI-2207053, EBI-2207093;
CC Q97SE5; Q97SR4: uppS; NbExp=2; IntAct=EBI-2207053, EBI-2206983;
CC Q97SE5; Q97QP2: xerS; NbExp=2; IntAct=EBI-2207053, EBI-2207218;
CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP-
CC Rule:MF_00122}.
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DR EMBL; AE005672; AAK74600.1; -; Genomic_DNA.
DR PIR; G95050; G95050.
DR RefSeq; WP_000705418.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97SE5; -.
DR SMR; Q97SE5; -.
DR IntAct; Q97SE5; 30.
DR STRING; 170187.SP_0438; -.
DR EnsemblBacteria; AAK74600; AAK74600; SP_0438.
DR KEGG; spn:SP_0438; -.
DR eggNOG; COG0721; Bacteria.
DR OMA; VTPMAMK; -.
DR PhylomeDB; Q97SE5; -.
DR BioCyc; SPNE170187:G1FZB-453-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
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: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; IPR003837; Asp/Glu-ADT_csu.
DR InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR PANTHER; PTHR15004; PTHR15004; 1.
DR Pfam; PF02686; Glu-tRNAGln; 1.
DR SUPFAM; SSF141000; SSF141000; 1.
DR TIGRFAMs; TIGR00135; gatC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..100
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C"
FT /id="PRO_0000105343"
SQ SEQUENCE 100 AA; 11055 MW; 2B3CC5B2ABA9F246 CRC64;
MKITQEEVTH VANLSKLRFS EEETAAFATT LSKIVDMVEL LGEVDTTGVA PTTTMADRKT
VLRPDVAEEG IDRDRLFKNV PEKDNYYIKV PAILDNGGDA
