ID   SYGB_PASMU              Reviewed;         689 AA.
AC   P57905;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   25-MAY-2022, entry version 125.
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=PM1102;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03186.1; -; Genomic_DNA.
DR   RefSeq; WP_010907018.1; NC_002663.1.
DR   AlphaFoldDB; P57905; -.
DR   SMR; P57905; -.
DR   STRING; 747.DR93_861; -.
DR   EnsemblBacteria; AAK03186; AAK03186; PM1102.
DR   KEGG; pmu:PM1102; -.
DR   PATRIC; fig|272843.6.peg.1115; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 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; Reference proteome.
FT   CHAIN           1..689
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072917"
SQ   SEQUENCE   689 AA;  76019 MW;  D67A980B5143B21E CRC64;
     MTTQNFLAEI GTEELPPKAL KKLATAFAEN MELELNQAGL AFESVQWFAA PRRLAVKVLA
     LATSQPSKEI EKRGPAVSAA FDAEGKPTKA AEGWARGCGI SVEQAERVAT DKGEWLVHRA
     TIEGQPTKNL LKDMVANALA KLPIPKPMRW ADKTVQFIRP VHTVTMLLGD ELIEGEILGV
     ESARTLRGHR FLGEREFQIS HADQYPALLK EKGSVVADFN DRKALILAKS QEKATALGGV
     ADIEDDLLDE VTSLVEYPNV LAAKFEERFL AVPAEALVYT MKGDQKYFPI YDKDGKLLPH
     FIFVSNINPD DPSKIIEGNE KVVRPRLTDA EFFFKTDLKQ RLEDQLPRLE TVLFQQQLGT
     LRDKTARIEQ LAGEIAKQIG ADEVKAKRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
     GEDEEVAVAL NEQYMPRFAG DELPKSLVAS AVALADKFDT LTGIFGIGQQ PKGSADPFAL
     RRAALGALRI IVEKNLPLDL AEIVKKSSAL FGDKLTNANV VEDVVEFMLG RFRAWYQDEG
     IAVDVIQAVL ARRPTKPSDF DARVRAVSHF RALEAAEALA AANKRVSNIL AKVEGELPAN
     IDTTLCAEAA EKVLAEQVIA LQAELAPLFA KGEYQVALDR LAALREPVDT FFDNVMVNAE
     NPQLRQNRLA ILNNLRNLFL QVADISLLQ