ID   SYGB_STRU0              Reviewed;         679 AA.
AC   B9DV92;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=SUB1435;
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J;
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA   Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA   Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA   Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(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; AM946015; CAR43106.1; -; Genomic_DNA.
DR   RefSeq; WP_015911754.1; NC_012004.1.
DR   AlphaFoldDB; B9DV92; -.
DR   SMR; B9DV92; -.
DR   STRING; 218495.SUB1435; -.
DR   PRIDE; B9DV92; -.
DR   EnsemblBacteria; CAR43106; CAR43106; SUB1435.
DR   KEGG; sub:SUB1435; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000000449; 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; Reference proteome.
FT   CHAIN           1..679
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000197223"
SQ   SEQUENCE   679 AA;  76268 MW;  D4A4CFE2A6CD4541 CRC64;
     MTKNLLLELG LEELPAYVVT KSEMQLGEKV ASFLKENRLS FESIQTFSTP RRLAVRVIGL
     AEKQEDLIED FKGPSKKIAL DENGEFSKAA QGFVRGKGLT TDAIEFRTIK GEEYVYVTKH
     ENGKDAEEVL KDIPSVLSSL TFPVSMHWAN HTFEYIRPVH TLTVLLDDNA LDLDFLDIHS
     GQKSRGHRFL GKEVTIENAN SYESDLKTVF VIVDPKERQQ MILDQIKAIE IAENVAVDID
     EDLLNEVLNL VEYPTAFMGT FDQKYLDVPE EVLVTSMKNH QRYFVVRDKN GHLLPNFISV
     RNGNSEYIEN VIKGNEKVLV ARLEDGEFFW KEDQKLNIED LVAKLANVTF HEKIGSLSEH
     MARTKVIASH LAEKVGLSDQ ERQALDRASQ IYKFDLLTGM VGEFDELQGI MGEKYALLAG
     ESAMVATAIR EHYLPNSAEG ALPESKVGAL LALADKLDTL LSFFSVDLIP SGSNDPYALR
     RATQGIVRIL EAFGWNIPMD ALVENCYQLP FESLTYTNKD QVMSFISARV DKMMGKAIPK
     DIRDAVLAST NYQVPQMLET AQALVSASQS QGYKTAVENL SRVFNLAEKA EQEPQINSDL
     FENDEEIALY KAIENLNLEG NAKEKVEQLF ALNDVIVNFF DHTMVMVEDV NVKNNRLALL
     SSLVSKAQTL AQFNLLNSK