ID   SYGB_STRSV              Reviewed;         679 AA.
AC   A3CQ05;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=SSA_1879;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(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; CP000387; ABN45260.1; -; Genomic_DNA.
DR   RefSeq; WP_011837424.1; NC_009009.1.
DR   RefSeq; YP_001035810.1; NC_009009.1.
DR   AlphaFoldDB; A3CQ05; -.
DR   SMR; A3CQ05; -.
DR   STRING; 388919.SSA_1879; -.
DR   PRIDE; A3CQ05; -.
DR   EnsemblBacteria; ABN45260; ABN45260; SSA_1879.
DR   KEGG; ssa:SSA_1879; -.
DR   PATRIC; fig|388919.9.peg.1784; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000002148; 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..679
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101359"
SQ   SEQUENCE   679 AA;  75614 MW;  E40E6E8A0C851531 CRC64;
     MVKNLLVELG LEEMPAYVVT PSMKQLRDKM GAFLTDHRLT FEKIEMFSTP RRLAVRVVGL
     ADKQSDLTED FKGPSKKIAL DADGNFTKAA EGFVRGKGLT VEDITFREIK GEEYVYVTKE
     EIGRPVEEII PAVTEVLQAL TFPVSMHWAN NTFEYIRPVH TLTVLLDEQA FDLDFLDIKS
     GRTSRGHRFL GKETEISSAD SYEDDLRAQF VIASPLERGD MIVEQIRALE EEHGVSIEID
     ENLLNEVLNL VEYPTAFLGN FDAKYLEVPE EVLVTSMKEH QRYFVVRDAE GKLLPHFISV
     RNGNAEHLEN VIKGNEKVLV ARLEDGEFFW REDQKLAIAD LVEKLSNVTF HEKIGSLAEH
     MERTGKIAAL LAKEAGLDAN ETADLARAAA IYKFDLLTGM VGEFDELQGI MGEKYALLAG
     ENAAVAAAIR EHYMPTSADG ELPDTKVGAV LALADKLDTI LSFFSVGLIP SGSNDPYALR
     RATQGVVRIL DKFGWNIDLA QLLGRLYGLK FDSLSYDNQE AVLDFFRARV EKMMDRSTPK
     DIVTAVLQST NFVVRDLVET AALLAEKAQE DNFKSAVESL SRVFNLAEKA QGQTAINPAL
     FENQEEKDLA AAIEKVELTS DLAANMDQLF ALSPVIDAFF DHTMVMAEDE AVRNNRLALL
     ASLTAKAGQL AQFNQINTK