ID   SYGB_BUCBP              Reviewed;         697 AA.
AC   P59573;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=bbp_126;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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; AE016826; AAO26860.1; -; Genomic_DNA.
DR   RefSeq; WP_011091261.1; NC_004545.1.
DR   AlphaFoldDB; P59573; -.
DR   SMR; P59573; -.
DR   STRING; 224915.bbp_126; -.
DR   EnsemblBacteria; AAO26860; AAO26860; bbp_126.
DR   GeneID; 56470670; -.
DR   KEGG; bab:bbp_126; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000000601; 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; Reference proteome.
FT   CHAIN           1..697
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072897"
SQ   SEQUENCE   697 AA;  81300 MW;  BAA591BFFECD245B CRC64;
     MKNTFLIEIE TEELPPKSLK AIAQSFNKQI IEKSKTYYLK YKQTKWFATP RRIAVMILDI
     NTSDTNFYLQ TKGPSIKNAF DKLGNPTSIM KFWMQKMNIK IHEITYLNTN KGSWVTCSKI
     TNKKSIQEIL IELCRLAIKN ISIPTFMKWS NNDIQFSRPV RNVIMLLNHE IIRNNVLGLE
     TNRLLSGHKF MTNNKIILNH AYQYPELLLN SGKVIADYDA RKHKIQKHAS IAAQSVNGIL
     KIKTTLLEEI TALVEWPTIL LATFKKRFLN LPQEILVHII EKKQRCLPIY STNNGTILNS
     FVVVSNIETS YPNNIVRGNE RVIHAQFVDA EFFFKKDTKK KLIDYKPLLK KIIFHDTLGT
     LLDKTHRIKK LITWISKFTH ANVNDCIRAA DLSKCDLVTN MTFEFPECQG IIGMYYALHD
     LEPKNIAIAI KEQYQPKFSK DNLPSNTISY SLALADKIDT LTGLFSINKN YNISEKDPFS
     LRRLATGIMR IIIKKNIHIN LYDLLEKSLK TYKKINNSDI ILKKEIQFLF NRIYSIYDKN
     KYNHSIIKSI LENNTKILTN IDPKIKAITY VFKNHPKILQ NLIITQKRVS NILKQFKENI
     SFNINMKTLE QIEEIKLIEQ LNIIEKKYKH PFSKETYISM MLTLNSFCQL IHEFFNKVMI
     NHKIVSIKNN RLAILFKIQN LFFTISNFSN ININITI