ID   SYGB_HELPH              Reviewed;         701 AA.
AC   Q1CSQ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=HPAG1_0953;
OS   Helicobacter pylori (strain HPAG1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=357544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPAG1;
RX   PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA   Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA   Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA   Gordon J.I.;
RT   "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT   pylori strain: evolution during disease progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
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; CP000241; ABF85020.1; -; Genomic_DNA.
DR   RefSeq; WP_000555246.1; NC_008086.1.
DR   AlphaFoldDB; Q1CSQ2; -.
DR   SMR; Q1CSQ2; -.
DR   PRIDE; Q1CSQ2; -.
DR   EnsemblBacteria; ABF85020; ABF85020; HPAG1_0953.
DR   KEGG; hpa:HPAG1_0953; -.
DR   HOGENOM; CLU_007220_2_2_7; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000008835; 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_1000006368"
SQ   SEQUENCE   701 AA;  80365 MW;  2FFDF10F810ACD55 CRC64;
     MHSDELLVEI LVEELPAQAL LNEYKEMPKK LHALLNKRAL EAGNIEIFYT PRRLCLLIKD
     FPLLTQETKE EFFGPPIKIA FNNEDKTQGL NALGLGFYQK LGLKDHQHFQ TAFKNNKEVL
     YHAKIHEKEP TKDLIMPIVL EFLEGLNFGK SMRWGNVEKS FIRPIHNICV LFNGENFNGI
     EVKEYGFKTK QATKVHRQEG FDFIEVDSPK AYFEVLEKNH VILDPKKREA KILQEIKELE
     TKHDIIVEID RDLLDEVVAI TEYPSALLGE FDKAFLKLPN EIITTSMKEN QRYFAVFDQK
     SQEESPTLHN GFIVVSNAIN KDKQKIIAGN QKVLKARLSD AVFFYENDLK KPLDNTPLES
     VVFVQGLGTL KDKMEREAII AQYLTQKYAP SLNMPLEKAL ELIGRAVKIA KADLLSEVVY
     EFSELQGIMG YYYALKQNEN ELVALSVKEQ YLPASENAPL PSSVFSAIVA LSLKLDSLFS
     LFSAGKIPSG SKDPFALRRL SFGLLKIVAH YGLEFDLKAD LKNLFEKVGV YQSFDLEILE
     KFLLERFHNL IDCNPSIIRS VLNTNERDIV KIIQKVKALK RFLDDPKNAQ KKELLFSAFK
     RLANINKDRN PNESSEFSIS LFKELQEHAL FEAFNAIQTS AFEGLDSKIE AYFGLHAPLE
     EYFKSVLVMD KDIEIQKNRK NFLWGVYQSF LEIGDIKEIA I