ID   SYGB_BUCAI              Reviewed;         690 AA.
AC   P57235;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Glycine--tRNA ligase beta subunit;
DE            EC=6.1.1.14;
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit;
DE            Short=GlyRS;
GN   Name=glyS; OrderedLocusNames=BU135;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(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;
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000003; BAB12853.1; -; Genomic_DNA.
DR   RefSeq; NP_239967.1; NC_002528.1.
DR   RefSeq; WP_009874091.1; NC_002528.1.
DR   AlphaFoldDB; P57235; -.
DR   SMR; P57235; -.
DR   STRING; 107806.10038818; -.
DR   EnsemblBacteria; BAB12853; BAB12853; BAB12853.
DR   KEGG; buc:BU135; -.
DR   PATRIC; fig|107806.10.peg.144; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000001806; 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..690
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072895"
SQ   SEQUENCE   690 AA;  80803 MW;  2788D93B7B231403 CRC64;
     MTKKILLIEI GTEELPARLL SKISLYFYKN FIKELDFHNI SYKNIKYFST PRRLALKIKD
     IDITERFVEI KKRGPSIINS YDKDGFLTEA ATRWLKHCGI NINQAIRLKN EKGEWLFYKT
     RKKQENIESL IPKITESALK NISIKKSMRW GQDNQKFSRP IRNIVILLDK KVIPGDVFNI
     TSKNLLQNHL SSKDSQIKIK DAKDYPKILL EKNNIIADYF IRKEKIIEDI ENIAKKIKGF
     IKKNNVLIEE VTALVESPKA LLVNFQEKFL QIPKKILINT IEKKQKCFPI YNSEKKLLPY
     FIFISNIQTQ ESEKIIIGNQ RVMHARLSDA EFFFKNDRKV KLESRLLSLK KVLFQNNLGS
     LYEKTLRIKL LIKWIAKYSS SDVEDSIRAA LLSKCDLVTD VVCEFPELQG KIGMYYALED
     KEKKDVATAL EEQYLPRFSG DKLPCTPIGC GLSIADKMDT LSGMFYIGNI PSSDKDPFAL
     RRLAIGIIRI ILEKNIPLNL EDLIKKSLSL YNKKNEDDLI LFDKMIKFFM IRLFHWYEET
     GYSAKIIKSV LSCKSIELID IHKKIQAISF FKKLKDSQSI ILSIKRISNI LAKEKEKING
     DINKKLMIEK EEIILFNNIE EFDNYTKNLF LEKKYNDILI KIKSFENPIY NFFKKVKIYH
     SDSKIRLNRL LLLSKLKKIF FKIADFSYLY