ID   SYGB_CLOD6              Reviewed;         688 AA.
AC   Q182B8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=CD630_24320;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(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; AM180355; CAJ69318.1; -; Genomic_DNA.
DR   RefSeq; WP_011861551.1; NZ_CP010905.2.
DR   RefSeq; YP_001088945.1; NC_009089.1.
DR   AlphaFoldDB; Q182B8; -.
DR   SMR; Q182B8; -.
DR   STRING; 272563.CD630_24320; -.
DR   EnsemblBacteria; CAJ69318; CAJ69318; CD630_24320.
DR   KEGG; cdf:CD630_24320; -.
DR   KEGG; pdc:CDIF630_02675; -.
DR   PATRIC; fig|272563.120.peg.2567; -.
DR   eggNOG; COG0751; Bacteria.
DR   OMA; LPIPKRM; -.
DR   PhylomeDB; Q182B8; -.
DR   BioCyc; PDIF272563:G12WB-2584-MON; -.
DR   Proteomes; UP000001978; 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..688
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101268"
SQ   SEQUENCE   688 AA;  78470 MW;  2346E232152665A6 CRC64;
     MKNYLLFEIG VEEMPSRFVG STLEQLKNNL SKLFDENRIA FDKINAYGTP RRLTLVVEGL
     SDRQNDLEEE IKGPAKKIAV DAENNLTKPA LGFIKSKGLS ESDIYFKQVG KEEYIFATIK
     QDGKETSEVL KDILPETIKS VVFPKAMRWG GKNLKFARPI RWIVALLNDK VLEFDLEGII
     SSNVTKGHRF LGESTIEVDS IEDYFEKLEK NYIVLDQNKR KEMIRKQCIE VANSLGGEVE
     FDEDLLEEVT YLVEYPTAFY GEFDVDYIKL PKEVVITPMK QHQRYFPVLK EGKLLPNFIA
     VRNGDSYRID NVKAGNEKVL EARLADALFF YREDTKRNLE SYIEKLKTVV FQVKLGTIYD
     KTLRLEKLSA DILDSLGLVD EKTDTIRAAK LSKADLVTGM VGEFDELQGF MGKEYAKVGG
     ENDVVSEAIF EHYLPRFAGD ILPKTNAGVA LSIADKLDSI AGFFAIGIQP TGSQDPYALR
     RQALGILSIL MDRKVAVDIK VLIEHALDNY SELDFDKEEV VEQIMNFFNE RVKNLFKDLG
     IRYDVVDAVL SSDINDVSDM HMRALELNNW LEKDELVEML TAFNRVSTLA QKAESDKIDE
     SLLKEDAEIK LYNEFKQVKI KVNELLKDKK YGIALDEFAS LRPVVDNLFD TVMVMDNDEA
     IKNNRLALLK QVYDTMLEIC DLSKIVYK