ID   SYGB_DESRM              Reviewed;         695 AA.
AC   A4J7C9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Dred_2472;
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) 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; CP000612; ABO50982.1; -; Genomic_DNA.
DR   RefSeq; WP_011878780.1; NC_009253.1.
DR   AlphaFoldDB; A4J7C9; -.
DR   SMR; A4J7C9; -.
DR   STRING; 349161.Dred_2472; -.
DR   PRIDE; A4J7C9; -.
DR   EnsemblBacteria; ABO50982; ABO50982; Dred_2472.
DR   KEGG; drm:Dred_2472; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000001556; 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..695
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101273"
SQ   SEQUENCE   695 AA;  77489 MW;  8618C7422B66D8E3 CRC64;
     MAKDFLLEVG IEEMPARFLG PALTQLKEQT VKTLQELRIE YADIQTYGTP RRLVLYIKDL
     AENQAALEKE VKGPAKKAAF DAAGNPTKAI LGFTRSQGVS MEDLVVRSIG QVEYLYALKR
     EEGRPTAQVL AEICPGLIAG LHFPKPMRWG ELELRFARPI RWLLALFGEA VVPFELANLQ
     SNRFTYGHRF LSTGDLSIAN PEDYFTKIRG AYVLIDPAER KELIWQQVQE LATAEGGVVE
     KDEDLLDEIT NILEWPTALC GTFDEDYLKL PGAVLVTPMR EHQRYFPVVS NEGKLLNKFI
     AVRNGTRAYI EIVTAGNEKV LRARLADAAF FFEEDLKQPL ASKVNGLQKV VFLEGLGSIA
     DKVDRIGAMA DHLAETLGAN EEQRENIQRG ALLAKADLIT NMVYEFPELQ GEMGREYALR
     NGEAPEVAEA IFEHYLPRFA GDLLPETLAG SVLSVADKMD SIVGCFAIGI QPTGSQDPYA
     LRRQALGICH MLIEGNIHLS LRELVQWAYQ GYHEGVELKQ DLNQVITEIE EFFKQRLKGI
     LNDRGLSYDT VDAVLTAGFD DIADVVDRGM ALAAFRELPA FAALMTAFNR ANNLAKHATT
     TQVQEVHLEH SAEQELYGLL TKLEGEVRPL LEQKNYALAL QKIATIQSPL DTFFESVMVM
     VEDEAVKTNR LALLKKLVGL SMNVADFSKI VVETK