ID   SYGB_NEIMB              Reviewed;         687 AA.
AC   Q9JXQ5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=NMB1930;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF42259.1; -; Genomic_DNA.
DR   PIR; E81027; E81027.
DR   RefSeq; NP_274924.1; NC_003112.2.
DR   RefSeq; WP_002244319.1; NC_003112.2.
DR   AlphaFoldDB; Q9JXQ5; -.
DR   SMR; Q9JXQ5; -.
DR   STRING; 122586.NMB1930; -.
DR   PaxDb; Q9JXQ5; -.
DR   EnsemblBacteria; AAF42259; AAF42259; NMB1930.
DR   KEGG; nme:NMB1930; -.
DR   PATRIC; fig|122586.8.peg.2458; -.
DR   HOGENOM; CLU_007220_2_2_4; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..687
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072916"
SQ   SEQUENCE   687 AA;  74573 MW;  616BCBDD76A3D4FB CRC64;
     MMTQTLLIEL LTEELPPKAL NNLGNHFAAS VAEGLEKAQL VDGAAEFTAY ASPRRLAVQV
     KNVKAVQADQ KIVKKGPAVA NAMKDGAPTK ALEGFARGAG AKIEDLTIVH DGKQDVYAYE
     YVQIGKPLGG LLEDIINQAV KKLPIPKVMR WGSSTFTFVR PVHGLVVLHG GDIVNVSVLG
     LQSGNKTLGH RFLSDGEITI ENADSYAAQM REQGKVVASF AERKAAIQTV LEGQARRLNA
     TAAADEALLD EVTALVEWPV VLEAGFEEHF LAVPQECLIL TMQQNQKYFP LLDQNGKLMN
     RFLLVSNLQT EDPSHIIQGN ERVLRARLSD AEFFYKQDQK ATLESRLPKL TNVVYHNKIG
     SQAERIERLQ SIAAHIAKAL GADAAAAERA ARLAKADLVT EMVGEFPELQ GTMGKYYARL
     DGETEEITEA VEQHYQPRFA GDNLPEGKIA AAVALADKLE TLVGIWGIGL IPTGDKDPYA
     LRRAALGILR MLMQYGLDVN ELIQTAFNSF PQGLLNEKTP SETADFMQAR LAVLLQNDYP
     QDIVAAVLAK QPRRLDDLTA KLQAVAAFKQ LPEAAALAAA NKRVQNLLKK ADAELGAVNE
     SLLQQDEEKA LFAAAQGLQP KIAAAVAEGN FQTALSELAS VKPQVDAFFD GVMVMAEDAA
     VKQNRLNLLN RLAEQMNAVA DIALLGE