ID   SYGB_TOLAT              Reviewed;         690 AA.
AC   C4L762;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=Tola_0008;
OS   Tolumonas auensis (strain DSM 9187 / TA4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Tolumonas.
OX   NCBI_TaxID=595494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA   Beller H.;
RT   "Complete sequence of Tolumonas auensis DSM 9187.";
RL   Submitted (MAY-2009) 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; CP001616; ACQ91638.1; -; Genomic_DNA.
DR   RefSeq; WP_012728238.1; NC_012691.1.
DR   AlphaFoldDB; C4L762; -.
DR   SMR; C4L762; -.
DR   STRING; 595494.Tola_0008; -.
DR   PRIDE; C4L762; -.
DR   EnsemblBacteria; ACQ91638; ACQ91638; Tola_0008.
DR   KEGG; tau:Tola_0008; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000009073; 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   SMART; SM00836; DALR_1; 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..690
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000204613"
SQ   SEQUENCE   690 AA;  75072 MW;  8B57AA3A1D4ADE4D CRC64;
     MATENFLIEL GTEELPPKAL RKLAQAFADN FTAELDKAGL AHQGVQWFAA PRRLALKVAA
     LADKQADKQV EKRGPAVSAA FDAAGNPTPA AAGWAKSNGI EVAQADRLAT DKGEWLVYRA
     NVAGQPTTGL LPAMAATALA GLPIPKPMRW GAKRTQFIRP VHTLCMLFGA ELVDGEILGL
     RSARIIRGHR FMGEAQFEIS HADQYPALLL EKGKVQADYE TRKAFIKAGA EAAAQQLGGI
     ADIEESLLEE VTSLVEWPVI LTATFEEKFL AVPAEALVHT MKGDQKYFPV YDNNGKLLPN
     FIFVSNIESK DPAQIIQGNE RVVRPRLSDA EFFFNTDKKH SLASRLESLD TVLFQQQLGT
     LKDKSVRIAE MSAFIAAQIG ADVEHATRAG LLSKCDLMTN MVMEFTDTQG VMGMHYARHD
     HEAEDVAVAL NEQYMPRFAG DNLPNGLVAC AVAIADKLDT LAGIFGIGQA PKGDKDPFAL
     RRAAIGTLRI IVEKQLDLDL VDVVSKAAEL YDGKISNKSV VDEVVDFMLG RFRASYQEAG
     IAVDVIQAVL ARRPTRPADF DARVKAVSHF RTLDAAEALA AANKRVSNIL AKFDGKLKDS
     VDAALLQDPA EQVLAQQVAA METKLAPLFA NGEYQLALTE LAALREAVDT FFDKVMVMAD
     DEALKLNRLT LLARLQALFL QAADISLLQQ