ID   SYGB_NEIM0              Reviewed;         687 AA.
AC   A9M127;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=NMCC_0288;
OS   Neisseria meningitidis serogroup C (strain 053442).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=374833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=053442;
RX   PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA   Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA   Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA   Liang X., Xu J., Jin Q.;
RT   "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT   clone.";
RL   Genomics 91:78-87(2008).
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; CP000381; ABX72496.1; -; Genomic_DNA.
DR   RefSeq; WP_012221229.1; NC_010120.1.
DR   AlphaFoldDB; A9M127; -.
DR   SMR; A9M127; -.
DR   PRIDE; A9M127; -.
DR   EnsemblBacteria; ABX72496; ABX72496; NMCC_0288.
DR   KEGG; nmn:NMCC_0288; -.
DR   HOGENOM; CLU_007220_2_2_4; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000001177; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 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..687
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101308"
SQ   SEQUENCE   687 AA;  74518 MW;  1240143CB8E833A8 CRC64;
     MMTQTLLIEL LTEELPPKAL NNLGNHFAAA VAEGLEKAQL VDGAAEFTAY ASPRRLAVQV
     KNVKAVQADQ KIVKKGPAVA NAMKDGAPTK ALEGFARGAG AKIEDLTIVH DGKQDVYAYE
     YVQTGKPLGE LLEDIINAAV KKLPIPKVMR WGSSTFTFVR PVHGLVVLHG GDIVNVSVLG
     LQSSNQTLGH RFLSNGEITI ENADSYAAQM REQGKVVASF AERKAAIQTA LEGQARRLNA
     SVAADEALLD EVTALVEWPV VLEAGFEEHF LAVPQECLIL TMQQNQKYFP LLDQNGKLMN
     RFLLVSNLQT EDPSHIIRGN ERVLRARLSD AEFFYKQDQK ATLESRLPKL SSVVYHNKIG
     SQAERIERLQ SIAAHIAKAL GADAAAAERA ARLAKADLVT EMVGEFPELQ GTMGKYYARL
     DGETEEIAEA VEQHYQPRFA GDNLPNGKVA TAVALADKLE TLVGIWGIGL IPTGDKDPYA
     LRRAALGILR MLMQYGLDVN ELIQTAFDSF PKGLLNEKTP SETADFMQAR LAVLLQNDYP
     QDIVAAVLAK QPRRLDDVVA KLQAVAAFKQ LPEAAALAAA NKRVQNLLKK ADAALGEVNE
     SLLQQDEEKA LFAAAQGLQP KIAAAVAEGN FQTALSELAS VKPQVDAFFD GVMVMAEDAA
     VKQNRLNLLN RLAEQMNAVA DIALLGE