ID   SYG_BACC1               Reviewed;         458 AA.
AC   Q72YG8;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Glycine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00253};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00253};
DE   AltName: Full=Glycyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00253};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00253};
GN   Name=glyQS {ECO:0000255|HAMAP-Rule:MF_00253}; Synonyms=glyS;
GN   OrderedLocusNames=BCE_5053;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
CC   -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly).
CC       {ECO:0000255|HAMAP-Rule:MF_00253}.
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_00253};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00253}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00253}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00253}.
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DR   EMBL; AE017194; AAS43954.1; -; Genomic_DNA.
DR   RefSeq; WP_000287154.1; NC_003909.8.
DR   AlphaFoldDB; Q72YG8; -.
DR   SMR; Q72YG8; -.
DR   EnsemblBacteria; AAS43954; AAS43954; BCE_5053.
DR   GeneID; 59157199; -.
DR   GeneID; 64204177; -.
DR   GeneID; 67469201; -.
DR   KEGG; bca:BCE_5053; -.
DR   HOGENOM; CLU_015515_2_1_9; -.
DR   OMA; EPSYGID; -.
DR   Proteomes; UP000002527; 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; ISS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00774; GlyRS-like_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_00253_B; Gly_tRNA_synth_B; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR   InterPro; IPR022961; Gly_tRNA_ligase_bac.
DR   InterPro; IPR033731; GlyRS-like_core.
DR   InterPro; IPR002315; tRNA-synt_gly.
DR   PANTHER; PTHR10745; PTHR10745; 3.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01043; TRNASYNTHGLY.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..458
FT                   /note="Glycine--tRNA ligase"
FT                   /id="PRO_0000072944"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         203..205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         213..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         218..222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         287..288
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         327..331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         331..334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
SQ   SEQUENCE   458 AA;  53018 MW;  47FB512781095788 CRC64;
     MYSMEQVVNL AKHRGFVFPG SEIYGGLANT WDYGPLGIEL KNNVKKAWWK KFIQESPYNV
     GLDAAILMNP KTWIASGHVG NFNDPMIDCK KCKARHRADK LIEDALDAKG IEMVVDGLTF
     DQMADLMKEH EVKCPDCGSE EFTEIRQFNL MFKTFQGVTE SSTNEIFLRP ETAQGIFVNF
     KNVQRSMRKK LPFGIGQIGK SFRNEITPGN FTFRTREFEQ MELEFFCKPG EDLEWFAFWR
     ETCKNWLLSL GMTEESMRLR DHGEEELSHY SNATTDIEFK FPFGWGELWG VASRTDFDLK
     RHMEHSNEDF NYIDPQTNER YVPYCIEPSL GADRVTLAFL CDAYEEEQLE NDSRTVLRFH
     PALAPYKAAI LPLSKKLSEG ATEVFAELAK DFMVDFDETG SIGKRYRRQD EIGTPFCITY
     DFDSVEDKAV TVRDRDTMEQ VRMPISELKG FLEKKIQF