GATA_BACSU
ID GATA_BACSU Reviewed; 485 AA.
AC O06491;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE Short=Glu-ADT subunit A;
DE EC=6.3.5.7;
GN Name=gatA; Synonyms=yedB, yerM; OrderedLocusNames=BSU06680;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC STRAIN=168;
RX PubMed=9342321; DOI=10.1073/pnas.94.22.11819;
RA Curnow A.W., Hong K.-W., Yuan R., Kim S.-I., Martins O., Winkler W.,
RA Henkin T.M., Soell D.;
RT "Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for
RT correct decoding of glutamine codons during translation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11819-11826(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-256.
RC STRAIN=168;
RX PubMed=8969499; DOI=10.1099/13500872-142-11-3027;
RA Borriss R., Porwollik S., Schroeter R.;
RT "The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a
RT region devoted to purine uptake and metabolism, and containing the genes
RT cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide
RT sequence.";
RL Microbiology 142:3027-3031(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-87.
RC STRAIN=168 / JH642;
RX PubMed=11902719; DOI=10.1046/j.1365-2958.1997.4441809.x;
RA von Blohn C., Kempf B., Kappes R.M., Bremer E.;
RT "Osmostress response in Bacillus subtilis: characterization of a proline
RT uptake system (OpuE) regulated by high osmolarity and the alternative
RT transcription factor sigma B.";
RL Mol. Microbiol. 25:175-187(1997).
RN [5]
RP INTERACTION WITH BRXC, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168 / CU1065 {ECO:0000303|PubMed:33722570};
RX PubMed=33722570; DOI=10.1016/j.redox.2021.101935;
RA Gaballa A., Su T.T., Helmann J.D.;
RT "The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr
RT (YpdA) disulfide reductase reduce S-bacillithiolated proteins.";
RL Redox Biol. 42:101935-101935(2021).
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).
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 -!- SUBUNIT: Heterotrimer of A, B and C subunits (PubMed:9342321).
CC Interacts with BrxC (PubMed:33722570). {ECO:0000269|PubMed:33722570,
CC ECO:0000269|PubMed:9342321}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000305}.
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; AF008553; AAB83964.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12488.1; -; Genomic_DNA.
DR EMBL; AF011545; AAB72184.1; -; Genomic_DNA.
DR EMBL; U92466; AAB66513.1; -; Genomic_DNA.
DR PIR; B69795; B69795.
DR PIR; T44452; T44452.
DR PIR; T51582; T51582.
DR RefSeq; NP_388550.1; NC_000964.3.
DR RefSeq; WP_003242878.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O06491; -.
DR SMR; O06491; -.
DR IntAct; O06491; 1.
DR MINT; O06491; -.
DR STRING; 224308.BSU06680; -.
DR jPOST; O06491; -.
DR PaxDb; O06491; -.
DR PRIDE; O06491; -.
DR EnsemblBacteria; CAB12488; CAB12488; BSU_06680.
DR GeneID; 938748; -.
DR KEGG; bsu:BSU06680; -.
DR PATRIC; fig|224308.179.peg.726; -.
DR eggNOG; COG0154; Bacteria.
DR InParanoid; O06491; -.
DR OMA; EVSCPHF; -.
DR PhylomeDB; O06491; -.
DR BioCyc; BSUB:BSU06680-MON; -.
DR BioCyc; MetaCyc:MON-13955; -.
DR PRO; PR:O06491; -.
DR Proteomes; UP000001570; 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;
KW Reference proteome.
FT CHAIN 1..485
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000105138"
FT ACT_SITE 79
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 178
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT CONFLICT 435..444
FT /note="GVPGISVPCG -> AYRESGAMR (in Ref. 1; AAB83964)"
FT /evidence="ECO:0000305"
FT CONFLICT 463..485
FT /note="STVYRVAHAFEQATDHHKAKPEL -> ALYTALLMHLNKQQTIIKQNLNCKG
FT (in Ref. 1; AAB83964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 52664 MW; FD4BDDAE54E09DCC CRC64;
MSLFDHKITE LKQLIHKKEI KISDLVDESY KRIQAVDDKV QAFLALDEER ARAYAKELDE
AVDGRSEHGL LFGMPIGVKD NIVTKGLRTT CSSKILENFD PIYDATVVQR LQDAEAVTIG
KLNMDEFAMG SSTENSAYKL TKNPWNLDTV PGGSSGGSAA AVAAGEVPFS LGSDTGGSIR
QPASFCGVVG LKPTYGRVSR YGLVAFASSL DQIGPITRTV EDNAFLLQAI SGVDKMDSTS
ANVDVPDFLS SLTGDIKGLK IAVPKEYLGE GVGKEARESV LAALKVLEGL GATWEEVSLP
HSKYALATYY LLSSSEASAN LARFDGIRYG YRTDNADNLI DLYKQTRAEG FGNEVKRRIM
LGTFALSSGY YDAYYKKAQK VRTLIKKDFE DVFEKYDVIV GPTTPTPAFK IGENTKDPLT
MYANDILTIP VNLAGVPGIS VPCGLADGLP LGLQIIGKHF DESTVYRVAH AFEQATDHHK
AKPEL
