ID   SYGB_RHILO              Reviewed;         718 AA.
AC   Q986B5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=mlr7435;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB53538.1; -; Genomic_DNA.
DR   RefSeq; WP_010914845.1; NC_002678.2.
DR   AlphaFoldDB; Q986B5; -.
DR   SMR; Q986B5; -.
DR   STRING; 266835.14026942; -.
DR   PRIDE; Q986B5; -.
DR   EnsemblBacteria; BAB53538; BAB53538; BAB53538.
DR   KEGG; mlo:mlr7435; -.
DR   PATRIC; fig|266835.9.peg.5937; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_1_5; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000000552; 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; 2.
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..718
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072922"
SQ   SEQUENCE   718 AA;  78611 MW;  6664029CFFA0C689 CRC64;
     MPDLLLELRS EEIPARMQRK AAGDLKKMLT DGLVEAGLTY EAAREYWTPR RLTLDIRGLT
     ARSKDIREEI KGPSTTAPEQ AVQGFLRKAG LSSVADAHVH SDPKKGDFYV AHISKPGRAA
     EEIIAQLVPG IIRNFPWPKS MRWGPASAKP GSLRWVRPLQ SVLCTFGPET EEPVVVDFEI
     DGIRSGNITY GHRFLAPGEI TVRRFDDYVS KLEAAKVVLD ADRRKEIILA DARNLAFANG
     LDLVEDEGLL EEVSGLVEWP VVLMGEFEEA FLAIPAEVIR LTIRANQKCF VTRPQGEGEA
     LSNRFILTSN IEARDGGKEI AHGNGKVVRA RLSDALYFWT TDQGDLPDLG QLEASAEKFG
     LDLNKPLDQR MARLDHLNVT FHAKLGTQGE RVERIRRLAE ELAPTVGADP VLAARAAVLA
     KADLQTEVVG EFPELQGAMG RKYALLQGEH PSVAAAIEEH YKPQGPSDYV PSDPVSVAVA
     LADKLDTLVG FWAIDEKPTG SKDPYALRRA ALGVVRILVE DRIQLRLSSI FASAGACYAG
     SGADQTRDLL AFFHDRLKVY LRDQGARHDL IDAVITPQSD DLLQIVRRVE ALGSFLDTED
     GKNLLAGTKR AANILAAEEK KKTAVAKTVE PALFKENAEK SLFAAVNQAE KQAGEAIQNE
     DFSAAMLALS ALREPVDSFF EGVLVNDEDL EVRANRLALL TRIRAATGQV ADFSKIAG