SYGB_SHIF8
ID SYGB_SHIF8 Reviewed; 689 AA.
AC Q0SY78;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=SFV_3982;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF05987.1; -; Genomic_DNA.
DR RefSeq; WP_001291774.1; NC_008258.1.
DR AlphaFoldDB; Q0SY78; -.
DR SMR; Q0SY78; -.
DR EnsemblBacteria; ABF05987; ABF05987; SFV_3982.
DR GeneID; 66672553; -.
DR KEGG; sfv:SFV_3982; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR BioCyc; SFLE373384:SFV_RS21940-MON; -.
DR Proteomes; UP000000659; 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..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006413"
SQ SEQUENCE 689 AA; 76797 MW; 5177D52EF7A741F2 CRC64;
MSEKTFLVEI GTEELPPKAL RSLAESFAAN FTAELDNAGL AHGTVQWFAA PRRLALKVAN
LAEAQPDREI EKRGPAIAQA FDAEGKPSKA AEGWARGCGI TVDQAERLTT DKGEWLLYRA
HVKGESTEAL LPNMVATSLA KLPIPKLMRW GASDVHFVRP VHTVTLLLGD KVIPATILGI
QSDRVIRGHR FMGEPEFTID NADQYPEILR ERGKVIADYE ERKAKIKADA EEAARKIGGN
ADLSESLLEE VASLVEWPVV LTAKFEEKFL AVPAEALVYT MKGDQKYFPV YANDGKLLPN
FIFVANIESK DPQQIISGNE KVVRPRLADA EFFFNTDRKK RLEDNLPRLQ TVLFQQQLGT
LRDKTDRIQA LAGWIAEQIG ADVNHATRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEAEDVAVAL NEQYQPRFAG DDLPSNPVAC ALAIADKMDT LAGIFGIGQH PKGDKDPFAL
RRAALGVLRI IVEKNLNLDL QTLTEEAVRL YGDKLTNANV VDDVIDFMLG RFRAWYQDEG
YTVDTIQAVL ARRPTRPADF DARMKAVSHF RTLEAAAALA AANKRVSNIL AKSDEVLSDR
VNASTLKEPE EIKLAMQVVV LRDKLEPYFA EGRYQDALVE LAELREPVDA FFDKVMVMVD
DKELRLNRLT MLEKLRELFL RVADISLLQ