SYGB_XYLFT
ID SYGB_XYLFT Reviewed; 722 AA.
AC Q87D45;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255}; OrderedLocusNames=PD_0841;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
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DR EMBL; AE009442; AAO28709.1; -; Genomic_DNA.
DR RefSeq; WP_004572844.1; NC_004556.1.
DR AlphaFoldDB; Q87D45; -.
DR SMR; Q87D45; -.
DR EnsemblBacteria; AAO28709; AAO28709; PD_0841.
DR GeneID; 58016385; -.
DR KEGG; xft:PD_0841; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000002516; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR PANTHER; PTHR30075; PTHR30075; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR TIGRFAMs; TIGR00211; glyS; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..722
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000072941"
SQ SEQUENCE 722 AA; 80122 MW; 6A6B3CC7578A4B6A CRC64;
MTELKPLLIE LGTEELPVNA LPNLSRAFFE GVLAGLERRG IVVDHGEAKS LSTPRRLAVL
LTAVAVEQPK QYRELFGPYL NTAFDTEGKP TKALEGFAAK CGVNWRTLER IRDTKGERFV
HRVVVPGERT DALLPGILTE AIAGMPIPKP MRWGAHEYLF ARPVHWLVML FGQDVVEAEI
MGVKAGRISR GHRFLYDKPV SLSGPQNYID VLQAAYVLVD PAARRARIVA EIEAVARQVG
GVARITEDNV AQVVNLVEWP SAVLCSFERV FLEVPQEALI QTMEVNQKFF PVLDSLGKLT
EKFIGIANIE SNDVAEVAKG YERVIRPRFS DAKFFFNEDL KQGLKAMGER LRTVTYHAKL
GTLADKVARV LVLAEAIAPQ IGVDPLLARR VALLSKNDLQ SRMVNEFPEL QGVAGHHYAL
ISGELPEVAM AIEDAYRPRF SGDEIARSPL GKVLGLAERL DTLACGFAVG MKPTGNKDPF
GLRRNALGLA RTIIESRFDL DLKVLLDQAS DWVAFATTIE QERHAQESVK QSKKEAAVKH
SVPQVSDEKS ARIEELYDFI VERLRGYYAD KGIPTTHFNA VAELKPVSLY DFHRRLDAIG
RFAALPEAEA LAVANKRIRN ILRKAEIKIP ASVDATLFDQ PAESGLLVAL EGVITDTRSA
LDCKNYVSVL TCLARLRPPI DEFFDKVMVN DENLMLRANR LALLQRLGEY LCCVAAIEHL
SN