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Database: UniProt
Entry: A0A0D6U587_LACRH
LinkDB: A0A0D6U587_LACRH
Original site: A0A0D6U587_LACRH 
ID   A0A0D6U587_LACRH        Unreviewed;        98 AA.
AC   A0A0D6U587;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C {ECO:0000256|HAMAP-Rule:MF_00122};
DE            Short=Asp/Glu-ADT subunit C {ECO:0000256|HAMAP-Rule:MF_00122};
DE            EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_00122};
GN   Name=gatC {ECO:0000256|HAMAP-Rule:MF_00122,
GN   ECO:0000313|EMBL:NVO87707.1};
GN   ORFNames=BGK71_04935 {ECO:0000313|EMBL:ASX16774.1}, CCE29_01900
GN   {ECO:0000313|EMBL:ART94836.1}, FOS38_02940
GN   {ECO:0000313|EMBL:MBB1163905.1}, H0N82_07680
GN   {ECO:0000313|EMBL:NZA04988.1}, HWN39_04240
GN   {ECO:0000313|EMBL:NVO87707.1}, PY91_02700
GN   {ECO:0000313|EMBL:OAU25251.1};
OS   Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=47715 {ECO:0000313|EMBL:NVO87707.1, ECO:0000313|Proteomes:UP000542889};
RN   [1] {ECO:0000313|EMBL:OAU25251.1, ECO:0000313|Proteomes:UP000078528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lrh22 {ECO:0000313|EMBL:OAU25251.1,
RC   ECO:0000313|Proteomes:UP000078528};
RA   Ceapa C., Ritari J.;
RT   "The variable regions of Lactobacillus rhamnosus genomes reveal the dynamic
RT   evolution of metabolic and host-adaptation repertoires.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ASX16774.1, ECO:0000313|Proteomes:UP000215843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LR5 {ECO:0000313|EMBL:ASX16774.1,
RC   ECO:0000313|Proteomes:UP000215843};
RA   Nam Y.-D., Kang J., Chung W.-H.;
RT   "Complete genome sequence of Lactobacillus rhamnosus LR5.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ART94836.1, ECO:0000313|Proteomes:UP000195731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B15 {ECO:0000313|EMBL:ART94836.1,
RC   ECO:0000313|Proteomes:UP000195731};
RA   Oh N.-S.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:MBB1163905.1, ECO:0000313|Proteomes:UP000551634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 7102 {ECO:0000313|EMBL:MBB1163905.1,
RC   ECO:0000313|Proteomes:UP000551634};
RA   Leeuwendaal N., Stanton C., O'Toole P.W., Beresford T.;
RT   "Annotated Genomes of Lactobacillus rhamnosus DPC 7102 and Lactobacillus
RT   paracasei DCP 7150.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:NVO87707.1, ECO:0000313|Proteomes:UP000542889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QC {ECO:0000313|EMBL:NVO87707.1,
RC   ECO:0000313|Proteomes:UP000542889};
RA   Yi H., Jin M.;
RT   "Lactobacillus rhamnosus QC,genome.";
RL   Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:NZA04988.1, ECO:0000313|Proteomes:UP000552935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMC0712 {ECO:0000313|EMBL:NZA04988.1,
RC   ECO:0000313|Proteomes:UP000552935};
RA   Marsh A.J., Azcarate-Peril M.A.;
RT   "Organ Donor 1.";
RL   Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00024799,
CC       ECO:0000256|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:0000256|ARBA:ARBA00000352, ECO:0000256|HAMAP-
CC         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:0000256|ARBA:ARBA00000924, ECO:0000256|HAMAP-
CC         Rule:MF_00122};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits.
CC       {ECO:0000256|ARBA:ARBA00011123, ECO:0000256|HAMAP-Rule:MF_00122}.
CC   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000256|ARBA:ARBA00010757,
CC       ECO:0000256|HAMAP-Rule:MF_00122}.
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DR   EMBL; CP021426; ART94836.1; -; Genomic_DNA.
DR   EMBL; CP017063; ASX16774.1; -; Genomic_DNA.
DR   EMBL; VLHP01000002; MBB1163905.1; -; Genomic_DNA.
DR   EMBL; JABXWP010000004; NVO87707.1; -; Genomic_DNA.
DR   EMBL; JACCKI010000004; NZA04988.1; -; Genomic_DNA.
DR   EMBL; JTIH01000002; OAU25251.1; -; Genomic_DNA.
DR   RefSeq; WP_005710356.1; NZ_WPCQ01000005.1.
DR   STRING; 47715.AWJ15_00940; -.
DR   GeneID; 69831525; -.
DR   eggNOG; COG0721; Bacteria.
DR   OMA; VTPMAMK; -.
DR   OrthoDB; 9813938at2; -.
DR   Proteomes; UP000078528; Unassembled WGS sequence.
DR   Proteomes; UP000195731; Chromosome.
DR   Proteomes; UP000215843; Chromosome.
DR   Proteomes; UP000542889; Unassembled WGS sequence.
DR   Proteomes; UP000551634; Unassembled WGS sequence.
DR   Proteomes; UP000552935; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.20.60; Glu-tRNAGln amidotransferase C subunit, N-terminal domain; 1.
DR   HAMAP; MF_00122; GatC; 1.
DR   InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR   InterPro; IPR003837; GatC.
DR   NCBIfam; TIGR00135; gatC; 1.
DR   PANTHER; PTHR15004:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR15004; UNCHARACTERIZED; 1.
DR   Pfam; PF02686; GatC; 1.
DR   SUPFAM; SSF141000; Glu-tRNAGln amidotransferase C subunit; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00122};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Transferase {ECO:0000313|EMBL:NVO87707.1}.
SQ   SEQUENCE   98 AA;  10807 MW;  B06CD1321539AF5F CRC64;
     MISKDSVAHV ASLAKLQFSE ADLEKYTGQL SEILDMVEQL ESVSTKDVPV TTQSIHLENV
     MRPDVAKPSE PVAELLKNVP TKKGTYIQVP AIIDKEED
//
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