ID   SYGB_STRP1              Reviewed;         679 AA.
AC   Q99YI4; Q48XC3;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 133.
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=SPy_1688, M5005_Spy1384;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK34443.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ52002.1; -; Genomic_DNA.
DR   RefSeq; NP_269722.1; NC_002737.2.
DR   AlphaFoldDB; Q99YI4; -.
DR   SMR; Q99YI4; -.
DR   STRING; 1314.HKU360_01436; -.
DR   PaxDb; Q99YI4; -.
DR   EnsemblBacteria; AAK34443; AAK34443; SPy_1688.
DR   KEGG; spy:SPy_1688; -.
DR   KEGG; spz:M5005_Spy1384; -.
DR   PATRIC; fig|160490.10.peg.1469; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000750; 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_0000072929"
SQ   SEQUENCE   679 AA;  74930 MW;  0C8A16B21B23B678 CRC64;
     MSKNLLIELG LEELPAYVVT PSEKQLGERL ATFLTENRLS FEDIQTFSTP RRLAVRVSGL
     ADQQTDLTED FKGPAKKIAL DADGNFSKAA QGFVRGKGLT TDAIEFREVK GEEYVYVTKH
     EAGKPAKEVL LGVTEVLSAM TFPVSMHWAN NSFEYIRPVH TLTVLLNDEA LELDFLDIHS
     GRVSRGHRFL GTETTITSAD SYEADLRSQF VIADAKERQE MIVEQIKTLE VEQGVQVDID
     EDLLNEVLNL VEFPTAFMGS FEAKYLDVPE EVLVTSMKNH QRYFVVRDQA GHLMPNFVSV
     RNGNDQAIEN VIKGNEKVLV ARLEDGEFFW REDQKLQIAD LVAKLTNVTF HEKIGSLAEH
     MDRTRVIAAS LAKEANLSAE EVTAVDRAAQ IYKFDLLTGM VGEFDELQGI MGEKYALLAG
     EDAAVATAIR EHYLPDAAGG ALPETKVGAV LALAAKLDTL LSFFSVGLIP SGSNDPYALR
     RATQGIVRIL DHFGWRIPMD KLVDSLYDLS FDSLTYANKA DVMNFIRARV DKMMGKAAPK
     DIREAILASS TFVVPEMLAA AEALVKASHT ENYKPAVESL SRAFNLAEKA DASVQVDPSL
     FENEQENTLF AAIQGLTLAG SAAQQLEQVF ALSPVINDFF DNTMVMAGDQ ALKNNRLAIL
     SDLVSKAKTI VAFNQLNTK