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SYGB_HELPJ
ID   SYGB_HELPJ              Reviewed;         701 AA.
AC   Q9ZKM9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=jhp_0906;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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; AE001439; AAD06479.1; -; Genomic_DNA.
DR   PIR; H71874; H71874.
DR   RefSeq; WP_000555287.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZKM9; -.
DR   SMR; Q9ZKM9; -.
DR   STRING; 85963.jhp_0906; -.
DR   PRIDE; Q9ZKM9; -.
DR   EnsemblBacteria; AAD06479; AAD06479; jhp_0906.
DR   KEGG; hpj:jhp_0906; -.
DR   PATRIC; fig|85963.30.peg.54; -.
DR   eggNOG; COG0751; Bacteria.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000804; 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_0000072907"
SQ   SEQUENCE   701 AA;  80358 MW;  8D46ACE618A7DF99 CRC64;
     MHSDELLVEV LVEELPAQAL LNEYKEMPKK LHALFQKRAL EVGNIEVFYT PRRLCLFVKD
     FPLLTQETKE EFFGPPVKIA CNNQDKTQGL NALGLGFYQK LGLKDHQHFQ TAFKSNKEVL
     YHAKIHAKQP TKDLIMPIVL EFLEGLNFGK SMRWGNVEKS FIRPIHNICV LFNGENFNDI
     EIKEYGFKTK QATKAHRQEG FDFIEVDSPK AYFEVLEKNH VILDPKKREA KILQEIKGLE
     KKHDIIVEVD RDLLDEVVAI TEYPTALLGE FDKAFLKLPS EIITTSMKEN QRYFAIFNQK
     SQEESPTLHN GFIVVSNAIS KDKQKIILGN QKVLKARLSD AVFFYENDLK KPLDNAPLES
     VVFVQGLGTL KDKMERESII AQYLTQKYIS SLSMPLEKAL ELISRAIQIA KADLLSEVVY
     EFSELQGIMG YYYALKQNEN ELVALSVKEQ YLPASENAPL PSSVFSSIVA LSLKIDSLFS
     LFSVGKIPSG SKDPFALRRL SFGLLKIIAH YGLEFDLKAD LKNLFEKVGV YQSFDLEVLE
     KFLLERFHNL IDCNLSIIRS VLNTNERDIV KIIQKVKALK RFLDNPKNAQ KKELLFSAFK
     RLANINKDRN PNESSGFSTS LFKELQEHAL FEAFNAIKTS TFESLDSKIE AYFGLHAPLE
     EYFKSVLVMD KDIEIQKNRK NFLWGVYQSF LEIGDIKEIA I
 
 
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