SYGB_PSEU5
ID SYGB_PSEU5 Reviewed; 684 AA.
AC A4VFG6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=PST_0009;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP77717.1; -; Genomic_DNA.
DR RefSeq; WP_011911260.1; NC_009434.1.
DR AlphaFoldDB; A4VFG6; -.
DR SMR; A4VFG6; -.
DR STRING; 379731.PST_0009; -.
DR PRIDE; A4VFG6; -.
DR EnsemblBacteria; ABP77717; ABP77717; PST_0009.
DR KEGG; psa:PST_0009; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000000233; 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..684
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006395"
SQ SEQUENCE 684 AA; 74904 MW; 55DA058276D83A81 CRC64;
MSALDFLVEL GTEELPPKAL AKLADAFCAG IEKGLKDAGL GFAKAQAYAA PRRLAVLVEQ
LATQQPDRSI NLDGPPMQAA FDAHGEPTQA ALGFARKCGV DLAEIDRSGP KLKFSRTIEG
QPATQLLPGI VEASLNDLPI PKRMRWAARK EEFVRPTQWL VMLFGEQVID CEILAQRAGR
ESRGHRFHSP GQVHISKPSS YLEDLRGAHV IADFAERREL IAKRVEQLAS EQNGSAIVPP
ALLDEVTALV EWPVPLVCSF EERFLEVPQE ALISTMQDNQ KYFCLLDTNG KLLPRFITVA
NIESKDPAQI VSGNEKVVRP RLTDAEFFFK QDKKQPLERF NDRLKNVVFQ AQLGTVFDKA
ERVSRLAGLI AERTGGDKAR AMRAGLLSKA DLATEMVGEF PEMQGIAGYY YALNEGEPED
VALALNEQYM PRGAGGELPS TLTGAAVAVA DKLDTLVGIF GIGMLPTGSK DPYALRRAAL
GVLRILIEKQ LDLNLVEAVN FAIGQFGTQV KSAGLADQVL EFIFDRLRAR YEDEGVDVAA
YLSVRAVQPG SALDFDQRVQ AVQAFRTLPE AEALAAANKR VSNLLAKFEA KLPEAVEPRW
FDNATEFSLY SALQQAEQAV QPLAAARQYR EALERLAHLR GPVDAFFEAV LVNAEDASVR
ANRYALLARL RGLFLGVADI SALG