SYGB_HELPY
ID SYGB_HELPY Reviewed; 701 AA.
AC P56454;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glycine--tRNA ligase beta subunit;
DE EC=6.1.1.14;
DE AltName: Full=Glycyl-tRNA synthetase beta subunit;
DE Short=GlyRS;
GN Name=glyS; OrderedLocusNames=HP_0972;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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;
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE000511; AAD08014.1; -; Genomic_DNA.
DR PIR; D64641; D64641.
DR RefSeq; NP_207763.1; NC_000915.1.
DR RefSeq; WP_000555186.1; NC_018939.1.
DR AlphaFoldDB; P56454; -.
DR SMR; P56454; -.
DR IntAct; P56454; 2.
DR STRING; 85962.C694_05005; -.
DR PaxDb; P56454; -.
DR EnsemblBacteria; AAD08014; AAD08014; HP_0972.
DR KEGG; hpy:HP_0972; -.
DR PATRIC; fig|85962.47.peg.1040; -.
DR eggNOG; COG0751; Bacteria.
DR OMA; LPIPKRM; -.
DR PhylomeDB; P56454; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR PANTHER; PTHR30075; PTHR30075; 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..701
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000072906"
SQ SEQUENCE 701 AA; 80635 MW; 70651DD7AD5F508B CRC64;
MHSDELLVEI LVEELPAQAL LNEYKEMPKK LHALFNKRAL EVGNIEIFYT PRRLCLLIKD
FPLLTQETKE EFFGPPVKIA CNHQDKTQGL NALGLGFYQK LGLKDHQYFQ TAFKNNKEVL
YHAKIHEKEP TKDLIMPIVL EFLEGLNFGK SMRWGNVEKS FIRPIHNICV LFNGEDFSGI
EVKEYGFKTK QATKVHRQEG FDFIQVDSPK AYFEVLEKNH VILDPKKREA KILQEIKELE
TKHHIIVETD RDLLDEVVAI TEYPSALLGE FDKAFLKLPS EIIITSMKEN QRYFATFCQK
SQEESPTLHN GFIVVSNAIN KDKQKIILGN QKVLKARLSD AVFFYENDLK KPLDNAPLES
VVFVQGLGTL KDKMERESII AQYLTQKYIS SLNMPLEKAL ELVKRAVQIA KADLLSEVVY
EFSELQGIMG YYYALKQNEN ELVALSVKEQ YLPASENAPL PSSVFSSIVA LSLKLDSLFS
LFSVGKIPSG SKDPFALRRL SFGLLKIIAH YGLEFDLKAD LKNLFQKVGV YQSFDLEILE
KFLLERFHNL IDCNPSIIRS VLNTNERDIV KIIQKVKALK RFLDDPKNAQ KKELLFSAFK
RLANINKDRN PNESSEFSTN LFKEPKEHAL FEAFNAIKMN AFESLDSKIE AYFGLHAPLE
EYFKSVLVMD KDIEIQKNRK NFLWGVYQSF LEIGDIKEIA I