ID   SYGB_STRZP              Reviewed;         678 AA.
AC   C1CLH4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-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=SPP_1495;
OS   Streptococcus pneumoniae (strain P1031).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=488223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1031;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000920; ACO20431.1; -; Genomic_DNA.
DR   RefSeq; WP_000164760.1; NC_012467.1.
DR   AlphaFoldDB; C1CLH4; -.
DR   SMR; C1CLH4; -.
DR   KEGG; spp:SPP_1495; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
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_1000197221"
SQ   SEQUENCE   678 AA;  75489 MW;  0D0CAB5DBDCE146B CRC64;
     MTKNLLVELG LEELPAYVVT PSEKQLGEKM AAFLKENRLS FEAIQTFSTP RRLAVRVTGL
     SDKQSDLTED FKGPAKKIAL DSDGNFTKAA QGFVRGKGLT VEDIEFREIK GEEYVYVTKE
     EVGQAVEAIV PGVVDVLKSL TFPVSMHWAG NSFEYIRPVH TLTVLLDEQE FDLDFLDIKG
     SRVSRGHRFL GKETKIQSAL SYEEDLRKQF VIADPCEREQ MIVDQIKEIE AKHGVRIEID
     ADLLNEVLNL VEYPTAFMGS FDAKYLEVPE EVLVTSMKEH QRYFVVRDQD GKLLPNFISV
     RNGNAERLKN 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 YFKPSVESLS RAFNLAEKAE GVATVDSALF
     ENDQEKALAE AVETLVLSGP ASQQLKQLFA LSPVIDAFFE NTMVMAEDQA VRQNRLAILS
     QLTKKAAKFA CFNQINTK