ID   SYGB_HELPS              Reviewed;         700 AA.
AC   B2UUB6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=HPSH_05135;
OS   Helicobacter pylori (strain Shi470).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=512562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shi470;
RA   Kersulyte D., Kalia A., Gilman R.H., Berg D.E.;
RT   "Genome sequence of Helicobacter pylori from the remote Amazon: traces of
RT   Asian ancestry of the first Americans.";
RL   Submitted (MAY-2008) 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; CP001072; ACD48448.1; -; Genomic_DNA.
DR   RefSeq; WP_000555183.1; NC_010698.2.
DR   AlphaFoldDB; B2UUB6; -.
DR   SMR; B2UUB6; -.
DR   KEGG; hps:HPSH_05135; -.
DR   HOGENOM; CLU_007220_2_2_7; -.
DR   OMA; LPIPKRM; -.
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..700
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101285"
SQ   SEQUENCE   700 AA;  80302 MW;  2F015C73E9589E6B CRC64;
     MHSDELLVEI LVEELPAQAL LNEYKEMPKK LHALFNKRAL EVGKIEIFYT PRRLCLLVKD
     FPLLTQETKE EFFGPPVKIA CNHQDKTQGL NELGLGFYQK LGLKDHQHFQ TAFKNNNEVL
     YHAKIHAKEP TKDLIMPIVL EFLEGLNFGK SMRWGNVEKS FIRPIHNICV LFNGENFNDI
     EVKEYGFKTK QATKAHRQEG FDFIQVDSPK AYFEVLEKNH VILDPKKRKA KILQEIKELE
     TKHRIIVEID RDLLDEVVAI TEYPSALLGE FDKAFLKLPN EIIITSMKEN QRYFAAFNQK
     SQESPTLHNG FIVVSNAISK DKQKIIAGNQ KVLKARLSDA VFFYENDLKK PLDNAPLESV
     VFVQGLGTLK DKMEREAIIA QYLTQKYASS LNMPLEKALE LVGRAVRIAK ADLLSEVVYE
     FSELQGIMGY YYALKQNENE LVALSVKEQY LPASENAPLP SSVFSAIVAL SLKLDSLFSL
     FSVGKIPSGS KDPFALRRLS FGLLKIVVHY GLEFDLKADL KNLFEKVGVY QSFDLEVLEK
     FLLERFNNLI DCNPSIIRSV LNTNERGIVK IIQKVKALKR FLDDPKNAQK KELLFSAFKR
     LANINKDRNP NESSEFFISL FKESQEHALF EAFNAIKTST FESLDSKIEA YFGLHAPLEE
     YFKSVLVMDK DIEIQKNRKN FLWGVYQSFL EIGDIKEIAI