GATC_STAAM
ID GATC_STAAM Reviewed; 100 AA.
AC P68807; Q9RF08;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C;
DE Short=Asp/Glu-ADT subunit C;
DE EC=6.3.5.-;
GN Name=gatC; OrderedLocusNames=SAV1901;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(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) (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;
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 -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000305}.
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DR EMBL; BA000017; BAB58063.1; -; Genomic_DNA.
DR RefSeq; WP_000170162.1; NC_002758.2.
DR PDB; 2DF4; X-ray; 3.20 A; C=1-100.
DR PDB; 2DQN; X-ray; 2.55 A; C=1-100.
DR PDB; 2F2A; X-ray; 2.30 A; C=1-100.
DR PDB; 2G5H; X-ray; 2.50 A; C=1-100.
DR PDB; 2G5I; X-ray; 3.35 A; C=1-100.
DR PDB; 3IP4; X-ray; 1.90 A; C=1-100.
DR PDBsum; 2DF4; -.
DR PDBsum; 2DQN; -.
DR PDBsum; 2F2A; -.
DR PDBsum; 2G5H; -.
DR PDBsum; 2G5I; -.
DR PDBsum; 3IP4; -.
DR AlphaFoldDB; P68807; -.
DR SMR; P68807; -.
DR PaxDb; P68807; -.
DR EnsemblBacteria; BAB58063; BAB58063; SAV1901.
DR GeneID; 66840130; -.
DR KEGG; sav:SAV1901; -.
DR HOGENOM; CLU_105899_1_2_9; -.
DR OMA; VTPMAMK; -.
DR PhylomeDB; P68807; -.
DR BioCyc; SAUR158878:SAV_RS10415-MON; -.
DR EvolutionaryTrace; P68807; -.
DR Proteomes; UP000002481; 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 3D-structure; ATP-binding; Ligase; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..100
FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT subunit C"
FT /id="PRO_0000105330"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 22..39
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:3IP4"
SQ SEQUENCE 100 AA; 11268 MW; 7E9273A6AA979250 CRC64;
MTKVTREEVE HIANLARLQI SPEETEEMAN TLESILDFAK QNDSADTEGV EPTYHVLDLQ
NVLREDKAIK GIPQELALKN AKETEDGQFK VPTIMNEEDA
