ID   SYGB_STRPD              Reviewed;         679 AA.
AC   Q1JFJ1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=MGAS10270_Spy1503;
OS   Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10270;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000260; ABF34568.1; -; Genomic_DNA.
DR   RefSeq; WP_020905394.1; NC_008022.1.
DR   AlphaFoldDB; Q1JFJ1; -.
DR   SMR; Q1JFJ1; -.
DR   EnsemblBacteria; ABF34568; ABF34568; MGAS10270_Spy1503.
DR   KEGG; sph:MGAS10270_Spy1503; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000002436; 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.
FT   CHAIN           1..679
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101351"
SQ   SEQUENCE   679 AA;  75020 MW;  9BD0FBC71979A982 CRC64;
     MSKNLLIELG LEELPAYVVT PSEKQLGERL ATFLTENRLS FEDIQTFSTP RRLAVRVSGL
     ADQQTDLTED FKGPAKKIAL DADGNFSKAA QGFVRGKGLT TDAIEFREVK GEEYVYVTKH
     EAGKPAKEVL LGVTEVLSAM TFPVSMHWAN NSFEYIRPVH TLTVLLNDEA LELDFLDIHS
     GCVSRGHRFL GTETTITSAD SYEADLRSQC VIVDAKERQE MIVEQIKTLE VEQGVQVDID
     ENLLNEVLNL VEFPTAFMGS FEAKYLDIPE EVLVTSMKNH QRYFVVRDQA GHLMPNFVSV
     RNGNDQAIEN VIKGNEKVLV ARLEDGEFFW REDQKLQIAD LVAKLTNVTF HEKIGSLAEH
     MDRTRVIAAS LAKEANLSAE EVTAVDRAAQ IYKFDLLTGM VGEFDELQGI MGEKYALLAG
     EDAAVATAIR EHYLPDAAGG ALPETKVGAV LALADKLDTL LSFFSVGLIP SGSNDPYALR
     RATQGIVRIL DHFGWRIPMD KLVDSLYDLS FDSLTYTNKA DVMNFIRARV DKMMGKAAPK
     DIREAILASS TFVVPEMLAV AEALVKASHT ENYKPAVESL SRAFNLAEKA DASVQVDPSL
     FENEQENTLF AAIQGLTLAG SAAQQLEQVF ALSPVINDFF DNTMVMAEDQ ALKNNRLAIL
     SDLVSKAKTI AAFNQLNTK