ID   SYGB_BRADU              Reviewed;         699 AA.
AC   Q89S69;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=blr2536;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC47801.1; -; Genomic_DNA.
DR   RefSeq; NP_769176.1; NC_004463.1.
DR   RefSeq; WP_011085323.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89S69; -.
DR   SMR; Q89S69; -.
DR   STRING; 224911.27350792; -.
DR   PRIDE; Q89S69; -.
DR   EnsemblBacteria; BAC47801; BAC47801; BAC47801.
DR   GeneID; 64022281; -.
DR   KEGG; bja:blr2536; -.
DR   PATRIC; fig|224911.44.peg.2116; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_1_5; -.
DR   InParanoid; Q89S69; -.
DR   OMA; LPIPKRM; -.
DR   PhylomeDB; Q89S69; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..699
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101266"
SQ   SEQUENCE   699 AA;  76434 MW;  C44E35239DE3E49E CRC64;
     MPDLLLELFS EEIPARMQAK AADDLRRMVT DKLVAEGLVY EGAKAFATPR RLALTVHGIP
     ARQPDLKTER RGPKMGAPDA AVQGFLKATG LKSLDEAKIQ RDPKGDFYIA LIEKPGRDAI
     DVLAEILPVI IRTFPWPKSM RWGARSGKPG SLNWVRPLHA ITATFGLETE EPDVVKFAVD
     GIEAGQTTYG HRFLAPAAIN VRRFEDYEAK LLDAKVVLDP ERRKDAILTD AKQLAFAQGF
     DLVEDQNLLD EVAGLVEWPV VLMGSFEEEF LATPAEVIRA TIRNNQKCFV VSDAKTGKLA
     NKFILVANIE ATDGGKTIIA GNERVIRARL SDAKFFYETD LKTKLEDRLP KFEQIVFHEE
     LGTQAARITR IERLAAEIAP LVGADVAKTA RAAHLAKADL LTEVVGEFPE VQGLMGKYYA
     LAQGEDASVA AACEEHYKPQ GPADRVPTDP VSVAVALADK LDTLVGFWAI DEKPTGSKDP
     YALRRAALGV IRLIAENTLR LSLMKVAASA LAGLSVKPAD VQKLPGDLLT FFADRLKVQL
     REQGARHDLV DAVFALGGQD DLLMIVRRVD ALGKFLESDD GKNLLAGTKR ASNILSIEEK
     KDKRTFDGAP DAALYSLGEE KALAKAISEV QAEASASVAK EDFAAAMSAM AKLRPPVDAF
     FDKVRVNDDD PKVRENRLKL LNEIRSATRA VADFSKIQD