ID   SYGB_STRE4              Reviewed;         679 AA.
AC   C0M9J7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=SEQ_0544;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204883; CAW92792.1; -; Genomic_DNA.
DR   RefSeq; WP_012679119.1; NC_012471.1.
DR   AlphaFoldDB; C0M9J7; -.
DR   SMR; C0M9J7; -.
DR   PRIDE; C0M9J7; -.
DR   EnsemblBacteria; CAW92792; CAW92792; SEQ_0544.
DR   KEGG; seu:SEQ_0544; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000001365; 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_1000197217"
SQ   SEQUENCE   679 AA;  75399 MW;  BA5574CB31A40ACA CRC64;
     MTKDLLVELG LEELPAYVVT PSEKQLVERM ADFLKANRLS YDAIEGFSTP RRLAVRVLGL
     ADQQTDLTED FKGPSKKIAL DADGQFSKAA QGFVRGKGLT VDDIEFREVK GEEYVYVTKH
     EAGKQAKDVL AAVPEVLASL TFPVSMHWAN NSFDYIRPVH SLIVLLDDEP LELDFLDIHS
     GRISRGHRFL GEETSITSAD SYEADLRSQF VIASAKERQE MIIAQIRAIE AEQKVQVDID
     EDLLNEVLNL VEYPTAFMGS FDPKYLEIPE EVLVTSMKNH QRYFVVRDQA GKLMPNFISV
     RNGNAKHLQN VIKGNEKVLV ARLEDGEFFW REDQKLSIED LVAKLAHVTF HEKIGSVAEH
     MERTKVIAAF LADQAGLSEA EKSAVARAAQ IYKFDLLTGM VGEFDELQGI MGEKYALLTG
     EAAAVATAIR EHYLPNSAEG ELPETKVGAV LALADKLDTL LSFFSVGLIP SGSNDPYALR
     RATQGIVRIL EHFGWSIPMD KLIDSLYELS FDSLTYQHKA EVLDFICARV DKMMGSAIPK
     DIREAVLASS SFVVPELLAR AEALAAASQL DTYKPAVESL SRVFNLAKKA VDAVLIDASL
     FENDYERALA QAVDSLVLSG SAKEQLAQVF ALSPVIDDFF DHTMVMTEDE AIRRNRLALL
     AELVKKVETI AAFDRLNTK