SYGB_HELPG
ID SYGB_HELPG Reviewed; 701 AA.
AC B5Z7X4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=HPG27_919;
OS Helicobacter pylori (strain G27).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27;
RX PubMed=18952803; DOI=10.1128/jb.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(2009).
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; CP001173; ACI27673.1; -; Genomic_DNA.
DR RefSeq; WP_000555189.1; NC_011333.1.
DR AlphaFoldDB; B5Z7X4; -.
DR SMR; B5Z7X4; -.
DR EnsemblBacteria; ACI27673; ACI27673; HPG27_919.
DR KEGG; hpg:HPG27_919; -.
DR HOGENOM; CLU_007220_2_2_7; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001735; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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.
FT CHAIN 1..701
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101284"
SQ SEQUENCE 701 AA; 80584 MW; 6A3248587BA3379D CRC64;
MHSDELLVEI LVEELPAQAL LNEYKEMPKK LHALFNKRAL EVGNIEIFYT PRRLCLLIKD
FPLLTQETKE EFFGPPVKIA CNNEDKTQGL NALGLGFYQK LGLKDHQHFQ TAFKNNKEVL
YHAKIHEKEP TKDLIMPIVL EFLEDLNFGK SMRWGNVEKS FIRPIHNICV LFNGENFNDI
EVKEYGFKTK QATKVHRQES FDFIEVDSPK AYFEVLEKNH VILDPKKREA KILQEIKELE
TEHHISIEID RDLLDEVVAI TEYPSALLGE FDKAFLKLPS EIITTSMKEN QRYFATFCQK
SQEESPTLHN GFIVVSNAIN KDKQKIILGN QKVLKARLSD AVFFYENDLK KPLDNAPLES
VVFVQGLGTL KDKMERESII AQYLTQKYAP SLNMPLEKAL ELVKRAVQIA KADLLSEVVY
EFSELQGIMG YYYALKQNEN ELVALSLKEQ YLPASENAPL PSSVFSAIVA LSLKLDSLFS
LFSVGKIPSG SKDPFALRRL SFGLLKIIAH YGLEFDLKAD LKSLFEKVGV YQSFDLEILE
KFLLERFNNL IDCNPSIIRS VLNTNERDIV KIIQKVKALK RFLDDPKNAQ KKELLFSAFK
RLANINKDRN PNESSEFSIS LFKESQEHAL FEAFNAIKTS AFEGLDSKIE AYFGLHAPLE
EYFKSVLVMD KDIEIQKNRK NFLWSVYQSF LEIGDIKEIA I
