ID   SYGB_THEMA              Reviewed;         672 AA.
AC   Q9WY60;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 130.
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=TM_0217;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AE000512; AAD35309.1; -; Genomic_DNA.
DR   PIR; C72404; C72404.
DR   RefSeq; NP_228032.1; NC_000853.1.
DR   RefSeq; WP_004082897.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WY60; -.
DR   SMR; Q9WY60; -.
DR   STRING; 243274.THEMA_03640; -.
DR   DNASU; 897102; -.
DR   EnsemblBacteria; AAD35309; AAD35309; TM_0217.
DR   KEGG; tma:TM0217; -.
DR   eggNOG; COG0751; Bacteria.
DR   InParanoid; Q9WY60; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   SUPFAM; SSF47323; SSF47323; 1.
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..672
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072934"
SQ   SEQUENCE   672 AA;  77813 MW;  612B402052DD429A CRC64;
     MRTALLEVGL EELPASEFHS ILKQLEEKSA ELLKAYRVSS GSVEVFVGSR RFGVILKNLP
     ERQEDFTEEK KGPPLNVAYD ENGKPTRALE GFLRNNNASL ENVVHREGYV YLSRVVEGKP
     VEEVLPDLFR DLVLGLNFRK PMRWGSGEHE YIRPVHWIVA MVDGRVLDLE IFGLRSSRIS
     YGKRYHAGSI EIPDSERYYE SLKKGFVISS HLERKKFVLE QIDEFEKRSS MKIERDEELI
     EEIVAITEYP RIVVGQFDRK YLELPEEIIV TAVKHHQRSF IAHKGTLTNT FVAFQDGPQP
     PENVVKGYER VINARLEDAR YYFQKDLETP LEKMNEKLKE IVFQEKLGTL YDKVERIKKI
     SQRLCEDLKL PGSFTQKVLE AASICKADIA SKVVYEFPEL QGVMGRIYAL REGINEEIAT
     AIEDHYSEEP QTVIGSILGI ADRIDTIVGN FAIGNVPTSS KDPYGLKSKA DTIFRIIRKN
     EWDISLEELL TFASSLVGYR LSEELETFFA GRFYQFLINE LGISFDVARA VNHLWKKPLR
     GILSAEALQE ISEKPEFQDL FVGFERVHNI TKNHDSTKFD GALFEKEEEK KLMNKFYEVK
     EKVLKALERL NYREALQYLI ELKPYIDEYF DNVFVMVKRD DLRVNRLSFL KNIDELFMMV
     GDMTYLVKRS QV