ID   SYGB_STRPS              Reviewed;         678 AA.
AC   B2IQU1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=SPCG_1463;
OS   Streptococcus pneumoniae (strain CGSP14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=516950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGSP14;
RX   PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA   Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT   "Genome evolution driven by host adaptations results in a more virulent and
RT   antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL   BMC Genomics 10:158-158(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; CP001033; ACB90715.1; -; Genomic_DNA.
DR   RefSeq; WP_000164752.1; NC_010582.1.
DR   AlphaFoldDB; B2IQU1; -.
DR   SMR; B2IQU1; -.
DR   EnsemblBacteria; ACB90715; ACB90715; SPCG_1463.
DR   KEGG; spw:SPCG_1463; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000001682; 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..678
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101356"
SQ   SEQUENCE   678 AA;  75386 MW;  21CAFE8E8DA0814A CRC64;
     MTKNLLVELG LEELPAYVVT PSEKQLGEKM AAFLKENRLS FEAIQTFSTP RRLAVRVTGL
     SDKQSDLTED FKGPAKKIAL DSDGNFTKAA QGFVRGKGLT VEDIEFREIK GEEYVYVTKE
     EVGQAVEAIV PGVVDVLKSL TFPVSMHWAG NSFEYIRPVH TLTVLLDEEE FDLDFLDIKG
     GRVSRGHRFL GQETKIQSAL SYEEDLRKQF VIADPCEREQ MIVDQIKTIE AERGVRIEID
     ADLLNEVLNL VEYPTAFMGS FDAKYLEVPE EVLVTSMKEH QRYFVVRDQD GKLLPNFISV
     RNGNAEHLEN VIKGNEKVLV ARLEDGEFFW REDQKLVISD LVEKLNNVTF HEKIGSLREH
     MIRTGQITVL LAEKAGLSVD ETVDLARAAA IYKFDLLTGM VGEFDELQGI MGEKYTLLAG
     ETPAVAAAIR EHYMPTSAEG ELPESKVGAV LAIADKLDTI LSFFSVGLIP SGSNDPYALR
     RATQGVVRIL DAFGWHIAMD ELIDSLYALK FDSLTYENKA EVMDFIKARV DKMMGSTPKD
     IKEAVLAGSN FVVADMLEAA SALVEVSKEE DFKPSVESLS RAFNLAEKAE GVATVDSALF
     ENDQEKALAE AVETLVLSGP ASQQLKQLFA LSPVIDAFFE NTMVMAEDQA VRQNRLAILS
     QLTKKAAKFA CFNQINTK