ID   SYGB_BUCAT              Reviewed;         690 AA.
AC   B8D740;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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};
GN   OrderedLocusNames=BUAPTUC7_134;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=561501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuc7;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
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; CP001158; ACL29955.1; -; Genomic_DNA.
DR   RefSeq; WP_012619444.1; NC_011834.1.
DR   AlphaFoldDB; B8D740; -.
DR   SMR; B8D740; -.
DR   PRIDE; B8D740; -.
DR   KEGG; bau:BUAPTUC7_134; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
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..690
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000197171"
SQ   SEQUENCE   690 AA;  80860 MW;  AC22B39C096AA6C1 CRC64;
     MTKKILLIEI GTEELPARLL SKISLYFYKN FIKELDFHNI SYKNIKYFST PRRLALKIKD
     IDITERFVEI KKRGPSIINS YDKDGFLTEA ATRWLKHCGI NINQAIRLKN EKGEWLFYKT
     RKKQENIESL IPKITESALK NISIKKSMRW GQDNQKFSRP IRNIVILLDK KVIPGDVFNI
     TSKNLLQNHL SLKDSQIKIK DAKDYPKILL EKNNIIADYF IRKEKIIEDI ENIAKKIKGF
     IKKNNVLIEE VTALVESPKA LLVNFQEKFL QIPKKILINT IEKKQKCFPI YNSEKKLLPY
     FIFISNIQTQ ESEKIIIGNQ RVMHARLSDA EFFFKNDRKV KLESRLLSLK KVLFQNNLGS
     LYEKTLRIKL LIKWIAKYSS SDVEDSIRAA LLSKCDLVTD VVCEFPELQG KIGMYYALED
     KEKKDVATAL EEQYLPRFSG DKLPCTLIGC GLSIADKMDT LSGMFYIGNI PSSDKDPFAL
     RRLAIGIIRI ILEKNIPLNL EDLIKKSLSL YNKKNEEDLI LFDKMIKFFM IRLFHWYEET
     GYSAKIIKSV LSCKSIELID IHKKIQAISF FKKLKDSQSI ILSIKRISNI LAKEKEKING
     DINKKLMIEK EEIILFNNIE EFDNYTKNLF LEKKYNDILI KIKSFENPIY NFFKKVKIYH
     SDSKIRLNRL LLLSKLKKIF FKIADFSYLY