ID   SYGB_NEIMF              Reviewed;         687 AA.
AC   A1KW08;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=NMC1903;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM421808; CAM11064.1; -; Genomic_DNA.
DR   RefSeq; WP_002256216.1; NC_008767.1.
DR   AlphaFoldDB; A1KW08; -.
DR   SMR; A1KW08; -.
DR   EnsemblBacteria; CAM11064; CAM11064; NMC1903.
DR   KEGG; nmc:NMC1903; -.
DR   HOGENOM; CLU_007220_2_2_4; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000002286; 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_1000101309"
SQ   SEQUENCE   687 AA;  74589 MW;  BC95A7E39E07AC8B CRC64;
     MTTQTLLIEL LTEELPPKAL NNLGNHFAAA VAEGLEKAQL VDGAAEFTAY ASPRRLAVQV
     KNVKAVQADQ KIVKKGPAVA NAVKDGAPTK ALEGFARGAG AKIEDLTIVH DGKQDVYAYE
     YVQTGKPLGG LLEDIINAAV KKLPIPKVMR WGSSTFTFVR PVHGLIVLHG GDIVNVSVLG
     LQSSNQTLGH RFLSNGEITI ENADSYAAQM REQGKVVASF AERKAAIQTA LEGQARRLNA
     TVAADEALLD EVTALVEYPV VLEAGFEEHF LAVPQECLIL TMQQNQKYFP LLDQNGKLMN
     RFLLVSNLQT EDPSHIIRGN ERVLRARLSD AEFFYKQDQK ATLESRLPKL ANVVYHNKIG
     SQAERIERLQ SIAAHIAKAL DADAAAAERA ARLAKADLVT EMVGEFPELQ GTMGKYYARL
     DGETEEIAEA IEQHYQPRFA GDKLPESKIA AAVALADKLE TLVGIWGIGL IPTGDKDPYA
     LRRAALGILR MLMQYGLDVN ELIQTAFDSF PKGLLNEKTP SETADFMQAR LAVLLQNDYP
     QDIVAAVLAK QPRRLDDLTA KLQAVAAFKQ LPEAAALAAA NKRVQNLLKK ADAELGEVNE
     SLLQQDEEKA LFAAAQGLQP KIAAAVAEGN FQTALSELAS VKPQVDAFFD GVMVMAEDAA
     VKQNRLNLLN RLAEQMNAVA DIALLGE