ID   SYGB_STRPF              Reviewed;         679 AA.
AC   Q1J5E1;
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=MGAS10750_Spy1495;
OS   Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10750;
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; CP000262; ABF38445.1; -; Genomic_DNA.
DR   RefSeq; WP_011528883.1; NC_008024.1.
DR   AlphaFoldDB; Q1J5E1; -.
DR   SMR; Q1J5E1; -.
DR   EnsemblBacteria; ABF38445; ABF38445; MGAS10750_Spy1495.
DR   KEGG; spi:MGAS10750_Spy1495; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000002434; 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_1000101352"
SQ   SEQUENCE   679 AA;  74973 MW;  BDB3FBA74C40F4CA CRC64;
     MSKNLLIELG LEELPAYVVT PSEKQLGERL ATFLTENRLS FEDIQTFSTP RRLAVRVSGL
     ADQQTDLTED FKGPAKKIAL DADGNFSKAA QGFVRGKGLT TDAIEFREVK GEEYVYVTKH
     EAGKPAKEVL LGVTEVLSAM TFPVSMHWAN NSFEYIRPVH TLTVLLNDEA LELDFLDIHS
     GRVSRGHRFL GTETTITSAD SYEADLRSQF VIADAKERQE MIVEQIKAIE AAQGVQVDID
     ADLLNEVLNL VEFPTAFMGS FDAKYLDVPE EVLVTSMKNH QRYFVVRDQE GHLMPNFVSV
     RNGNDQAIEN VIKGNEKVLV ARLEDGEFFW REDQKLQIAD LVAKLTNVTF HEKIGSLAEH
     MDRTRVIAAS LAKEANLSAE EVTAVDRAAQ IYKFDLLTGM VGEFDELQGI MGEKYARLAG
     EDAAVATAIR EHYLPDAAGG ALPETKVGAV LALADKLDTL LSFFSVGLIP SGSNDPYALR
     RATQGIVRIL DHFGWRIPMD KLVDSLYDLS FDSLTYANKA DVMNFIRARV DKMMGKAVPK
     DIREAVLESS TFVVPEMLAA AEALVKASHT ENYKPAVESL SRAFNLAEKA DASVQVDPSL
     FENEQENTLF AAIQGLTLAG SAAQQLEQVF ALSPVINDFF DNTMVMAEDQ ALKNNRLAIL
     SDLVSKAKAI AAFNQLNTK