SYGB_STRA3
ID SYGB_STRA3 Reviewed; 679 AA.
AC Q8CX30;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=gbs0260;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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; AL766844; CAD45905.1; -; Genomic_DNA.
DR RefSeq; WP_000159092.1; NC_004368.1.
DR AlphaFoldDB; Q8CX30; -.
DR SMR; Q8CX30; -.
DR STRING; 211110.gbs0260; -.
DR PRIDE; Q8CX30; -.
DR EnsemblBacteria; CAD45905; CAD45905; CAD45905.
DR KEGG; san:glyS; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000000823; 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..679
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101344"
SQ SEQUENCE 679 AA; 76610 MW; A3E0A5C98EE0E6FE CRC64;
MTKDLLLELG LEELPAYVVT PSEKQLGQKM VKFLEDHRLS FETVQTFSTP RRLAVRVKGL
ADQQTDLTED FKGPSKKIAL DAEGNFSKAA QGFVRGKGLS VDDIEFREVK GEEYVYVTKH
ETGKSAIDVL ASVTEVLTEL TFPVNMHWAN NSFEYIRPVH TLVVLLDDQA LELDFLDIHS
GRISRGHRFL GSDTEILSAS SYEDDLRQQF VIADAKERQQ MIVDQIHAIE EKENISVEID
EDLLNEVLNL VEYPTAFLGS FDEKYLDVPE EVLVTSMKNH QRYFVVRDRD GKLLPNFISV
RNGNAEHIEN VIKGNEKVLV ARLEDGEFFW QEDQKLNIAD LVEKLKQVTF HEKIGSLYEH
MDRVKVISQY LAEKADLSDE EKLAVLRAAS IYKFDLLTGM VDEFDELQGI MGEKYALLAG
EQPAVAAAIR EHYMPTSADG ELPETRVGAI LALADKFDTL LSFFSVGLIP SGSNDPYALR
RATQGIVRIL EAFGWDIPLD ELVTNLYGLS FASLDYANQK EVMAFISARI EKMIGSKVPK
DIREAVLESD TYIVSLILEA SQALVQKSKD AQYKVSIESL SRAFNLAEKV THSVSVDYSL
FENNQEKALY QAILSLELTE DMHDNLDKLF ALSPIINDFF DNTMVMTDDE KMKQNRLALL
NSLVAKARTV AAFNLLNTK