ID   SYGB_STRGC              Reviewed;         679 AA.
AC   A8AVS5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=SGO_0569;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV10025.1; -; Genomic_DNA.
DR   RefSeq; WP_012000066.1; NC_009785.1.
DR   AlphaFoldDB; A8AVS5; -.
DR   SMR; A8AVS5; -.
DR   STRING; 467705.SGO_0569; -.
DR   EnsemblBacteria; ABV10025; ABV10025; SGO_0569.
DR   KEGG; sgo:SGO_0569; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000001131; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 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..679
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101346"
SQ   SEQUENCE   679 AA;  75680 MW;  12B74653B4A596E8 CRC64;
     MVKNLLVELG LEEMPAYVVT PSMKQLRDKM GAFLTDHRLT FEKIEMFSTP RRLAVRVVGL
     ADKQSDLTED FKGPSKKIAL DADGNFTKAA EGFVRGKGLT VEDITFREIK GEEYVYVTKE
     EIGRPVEEII PAVTEVLQAL TFPVSMHWAN NTFEYIRPVH TLTVLLDEQA FDLDFLDIKS
     GRTSRGHRFL GQETEIASAD SYEDDLRAQF VIASPLERGD MIVDQIQALE EEHGVSIEID
     EDLLNEVLNL VEYPTAFLGN FDAKYLEVPE EVLVTSMKEH QRYFVVRDSE GKLLPHFISV
     RNGNAEHLEN VIKGNEKVLV ARLEDGEFFW REDQKLAIAD LVEKLNNVTF HEKIGSLAEH
     MERTGKIAAL LAQEAGLDAD ETADLARAAA IYKFDLLTGM VGEFDELQGI MGEKYALLAG
     ENAAVAAAIR EHYMPTSADG ELPDTKVGAV LALADKLDTI LSFFSVGLIP SGSNDPYALR
     RATQGVVRIL DKFGWNIDLA QLLGRLYELK FDSLSYDNQE AVLDFFRARV EKMMDRSIPK
     DIVTAVLQST HFVVRDLVET AALLAEKAQE DNFKSAVESL SRVFNLAEKA QGQTAVNPAL
     FENKEEKDLA AAIEKVVLTS DLAANLDQFF ALSPVIDAFF DHTMVMAEDE AVRNNRLALL
     ASLTAKAGQI AQFNQINTK