SYGB_NEIG1
ID SYGB_NEIG1 Reviewed; 687 AA.
AC Q5F4Y7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=NGO2154;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; AE004969; AAW90750.1; -; Genomic_DNA.
DR RefSeq; WP_010951416.1; NC_002946.2.
DR RefSeq; YP_209162.1; NC_002946.2.
DR AlphaFoldDB; Q5F4Y7; -.
DR SMR; Q5F4Y7; -.
DR STRING; 242231.NGO_2154; -.
DR EnsemblBacteria; AAW90750; AAW90750; NGO_2154.
DR KEGG; ngo:NGO_2154; -.
DR PATRIC; fig|242231.10.peg.2602; -.
DR HOGENOM; CLU_007220_2_2_4; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000000535; 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; Reference proteome.
FT CHAIN 1..687
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101306"
SQ SEQUENCE 687 AA; 74451 MW; BE39A8066422A986 CRC64;
MTTQTLLIEL LTEELPPKAL NNLGNHFAAS VAEGLEKAQL VDGAAEFTAY ASPRRLAVQV
KNVKAVQADQ KIVKKGPAVA NAVKDGTPTK ALEGFARGAG AKIEDLTIVH DGRQDVYAYE
YVQTGRPLGG LLENIINQAV KKLPIPKVMR WGSSTFTFVR PVHGLIVLHG GDVVNVSVLG
LQSGNQTLGH RFLSDGEIII ENADSYAAQM RGQGKVVASF AGRKAAIQTA LEGQARRLNA
TVAADEALLD EVTALVEWPV VLEAGFEEHF LAVPQECLIL TMQQNQKYFP LLDQNGKLMN
RFLLVSNLQT EDPSHIIRGN ERVLRARLSD AEFFYKQDQK ATLESRLPKL ANVVYHNKIG
SQAERIERLQ SIAAHIAKAL GADAAAAERA ARLAKADLVT EMVGEFPELQ GTMGKYYARL
DGETEEIAEA IEQHYQPRFA GDKLPESKIA AAVALADKLE TLVGIWGIGL IPTGDKDPYA
LRRAALGILR MLMQYGLDVN ELIQTAFDSF PQGLLNEKTP SETADFMQAR LAVLLQNDYP
QDIVAAVLAK QPRRLDDLTA KLQAVAVFKQ LPEAAALAAA NKRVQNLLKK ADAELGAVNE
SLLQQDEEKA LYAAAQGLQP KIAAAVAEGN FQTALSELAS VKPQVDAFFD GVMVMAEDAA
VKQNRLNLLN RLAGQMNAVA DIALLGE