ID   SYGB_THEP1              Reviewed;         672 AA.
AC   A5IKK4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=Tpet_0707;
OS   Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS   RKU-1).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-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; CP000702; ABQ46727.1; -; Genomic_DNA.
DR   RefSeq; WP_011943311.1; NC_009486.1.
DR   AlphaFoldDB; A5IKK4; -.
DR   SMR; A5IKK4; -.
DR   STRING; 390874.Tpet_0707; -.
DR   EnsemblBacteria; ABQ46727; ABQ46727; Tpet_0707.
DR   KEGG; tpt:Tpet_0707; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_0; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000006558; 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   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.
FT   CHAIN           1..672
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000006418"
SQ   SEQUENCE   672 AA;  77974 MW;  27CC04145417743F CRC64;
     MRTALLEVGL EELPASEFHS ILKQLEERST ELLKAYRISS GSAEVFVGSR RFGVILKNLP
     ERQEDFTEEK KGPPLNVAYD ENGKPTKALE GFLRNNNASL ENVVHREGYI YLSRVVEGKP
     VEEVLPDLFR DLVLGLNFRK PMRWGSGEHE YIRPVHWIVA MVDGRVLDLE IFGLRSSRIS
     YGKRYHAGSI KIPDPERYYE SLKKGFVISS HLERKKFVLE QIDEFEKRSG MKIERDEELI
     EEIVAITEYP RIVVGQFDRK YLELPEEIIV TAVKHHQRSF IAHKETLTNT FVAFQDGPQP
     PENVVKGYER VINARLEDAR YYFQKDLETP LEKMNEKLKE IVFQEKLGTL YDKVERIKKI
     SERLCEDLKL PESFTQKVLE AASICKADIA SKVVYEFPEL QGVMGRIYAL REGINEEIAT
     AIEDHYSEEP QTVIGSILGI ADRIDTIVGN FAIGNVPTSS KDPYGLKNKA DAIFRIIRKN
     EWDISLEELL TFASSLVGYR LSEELETFFA GRFYQFLVNE LGISFDVARA VNHLWKRPLR
     GILSAEALQE ISEKPEFQDL FVGFERVHNI TKNHDSVRFD GALFEKEEEK KLMNKFYEVK
     EKVLKALERL NYREALQYLI ELKPYIDEYF DNVFVMVKRD DLRVNRLGFL KNIDELFMMV
     GDMTYLVKRS QV