ID   SYGB_BUCAP              Reviewed;         691 AA.
AC   Q8KA07;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=BUsg_127;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(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; AE013218; AAM67695.1; -; Genomic_DNA.
DR   RefSeq; WP_044006080.1; NC_004061.1.
DR   AlphaFoldDB; Q8KA07; -.
DR   SMR; Q8KA07; -.
DR   STRING; 198804.BUsg_127; -.
DR   PRIDE; Q8KA07; -.
DR   EnsemblBacteria; AAM67695; AAM67695; BUsg_127.
DR   KEGG; bas:BUsg_127; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000000416; 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..691
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072896"
SQ   SEQUENCE   691 AA;  81070 MW;  B0138955825499EB CRC64;
     MIKKTFLVEI GTEELPSNIL KKIILVFYKN FVDELSFNKI LYKNINYFST PRRLALQIIE
     LDTSEKINEK IKKGPAIKHA FDENGNPTKA AYYWAKSCKI NLNQAERLKT KTGEWIIHRI
     QEKKEKIELL FPKIIEKILK QINLKNTMRW ETTNLRFIRP IRNIVMLLDE KIIKSEVFNV
     PSNNFLYHHI SCKEEKIYIK NAIEYPAVLF KKNKIIANYE TRKEKIKYEA KKIAKKVDGI
     IKTNPFLLEE VTSLVESPQA LLARFKKDYI NYIPKKILIH TIEKQQRCFS IYSNNSKKEI
     LPYFIFISNI KSKKNKEIIL GNEKVMHARL SDAMFFLKQD RKRKLENYLP FLKKVSFYNN
     LGTLYEKTLR LKLLIESISC YTNTINKNDL IRSAVLSKCD LITQMVDEFP ELQGTIGMYY
     ALENKENKEV AIAIKEQYLP SFSGDELPST PIGCLLSISD KIDTLSGMFA IGETPTPEKD
     PFGLRRAALG ILRIIITKKI PIDLKKIIEI SLKIYTFKKV NYSIISKKII KFFISRLSFF
     YEKKGYSTKV IKSVLSCKLT EPLDIDKRIN AISDLKKIES IILIAKRIDN IVKNNHQIIS
     SEIHVELMKK TEEKNLLKEI KIFNSKTKEL FIQKKYKEIL VEIKKLEKPI DNFFDKVQIN
     HSNFEIRQNR LLLLIKIQKF FLKIANFSYL Y