SYGB_PSEPG
ID SYGB_PSEPG Reviewed; 683 AA.
AC B0KF22;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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};
GN OrderedLocusNames=PputGB1_0076;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-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., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) 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; CP000926; ABY95992.1; -; Genomic_DNA.
DR RefSeq; WP_012269868.1; NC_010322.1.
DR AlphaFoldDB; B0KF22; -.
DR SMR; B0KF22; -.
DR STRING; 76869.PputGB1_0076; -.
DR PRIDE; B0KF22; -.
DR EnsemblBacteria; ABY95992; ABY95992; PputGB1_0076.
DR KEGG; ppg:PputGB1_0076; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000002157; 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.
FT CHAIN 1..683
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000078544"
SQ SEQUENCE 683 AA; 74966 MW; 5B1E5B49CE670EEB CRC64;
MSAQDFLVEL GTEELPPKAL ASLGDAFLAG IEKGLQAAGL NYTGKQVYAA PRRLAVLIRQ
LDVQQPDRSI NIDGPPMQAA FKDGEPTQAA LGFAKKCGVE LAEIDQSGAK LRFSQHIPGK
ATASLLPTII EDSLNDLPIP KRMRWAASRE EFVRPTQWLV MLLGDQVVDC TILSQKAGRE
SRGHRFHHPE NVVITTPANY VEDLRKAYVL ADFAERRELI SKRTAELAMQ QEGTAIVPPA
LLDEVTALVE WPVPLVCSFE ERFLEVPQEA LITTMQDNQK YFCLLDSEGK LLPRFITVAN
VESRDPKQIV QGNEKVVRPR LTDAEFFFKQ DKKQPLETFN ERLKNVVFQA QLGTVYDKAE
RVSKLAAFIA PLIGGDAQRA GRAGLLSKCD LATEMVGEFP EMQGVAGYYY ALNDGEPQDV
ALALNEQYMP RGAGAELPQT LTGAAVAIAD KLDTLVGIFG IGMLPTGSKD PYALRRAALG
VLRILIEKQL DLNLTGAVEF AVKQFGAKVK AAGLAEQVLE FIFDRLRARY EDEGIDVATY
LSVRALQPGS ALDFDQRVQA VQAFRKLPEA EALAAVNKRV SNLLSKAEGA IAEQVEPKYF
DNANEFSLYS AIQQADQAVQ PMAAARQYSE SLARLAALRD PVDAFFEAVM VNAEDAKVRA
NRYALLSRLR GLFLGVADIS LLG