ID   SYGB_HELP2              Reviewed;         701 AA.
AC   B6JMJ2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-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=HPP12_0968;
OS   Helicobacter pylori (strain P12).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=570508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12;
RA   Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT   "The complete genome sequence of Helicobacter pylori strain P12.";
RL   Submitted (OCT-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; CP001217; ACJ08120.1; -; Genomic_DNA.
DR   RefSeq; WP_000555239.1; NC_011498.1.
DR   AlphaFoldDB; B6JMJ2; -.
DR   SMR; B6JMJ2; -.
DR   EnsemblBacteria; ACJ08120; ACJ08120; HPP12_0968.
DR   KEGG; hpp:HPP12_0968; -.
DR   HOGENOM; CLU_007220_2_2_7; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000008198; 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_1000101283"
SQ   SEQUENCE   701 AA;  80354 MW;  3D1C0BD5829021D3 CRC64;
     MHSDELLVEI LVEELPAQAL LNEYKEMPKK LHALFQKRAL EVGTIEVFYT PRRLCLLIKD
     FPLLTQETKE EFFGPPVKIA CNHQDKMQGL NALGLGFYQK LGLKDHQHFQ TAFKNNKEVL
     YHAKIHAKEP TKDLIMPIVL EFLEGLNFGK SMRWGNVEKS FIRPIHNICV LFNGENFNNI
     EVKEYGFKTK QATKTHRQEG FDFIQVDSPK AYFEVLEKNH VILDPKKRKA KILQEIKELE
     TKHHIIVEID RDLLDEVVAI TEYPSVLLGE FDKAFLKLPS EIITTSMKEN QRYFAVFSQK
     SQEESPTLHN GFIVVSNAIS KDKQKIIAGN QKVLKARLSD AVFFYENDLK KPLDNAPLES
     VVFVQGLGTL KDKMERESTI AQYLTQKYAP SLNMPLEKAL ELIGRAVKIA KADLLSEVVY
     EFSELQGIMG YYYALKQNEN ELVALSLKEQ YLPASENAPL PSSVFSAIVA LSLKLDSLFS
     LFSVGKIPSG SKDPFALRRL SFGLLKIIAH YGLEFDLKAD LKNLFEKVGI YQSFDLEILE
     KFLLERFNNL IDCNPSIIRS VLNTNERDIV KIIQKVKALK RFLDDPKNAQ KKELLFSAFK
     RLANINKDRN PNESSGFSIS LFKELQEHAL FEAFNAIKTS AFESLDSKIE AYFGLHAPLE
     EYFKSVLVMD KDIEIQKNRK NFLWGVYQSF LEIGDIKEIA I