SYGB_STRPJ
ID SYGB_STRPJ Reviewed; 678 AA.
AC B8ZL20;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-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}; OrderedLocusNames=SPN23F14390;
OS Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=561276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700669 / Spain 23F-1;
RX PubMed=19114491; DOI=10.1128/jb.01343-08;
RA Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C.,
RA Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D.,
RA Mitchell T.J.;
RT "Role of conjugative elements in the evolution of the multidrug-resistant
RT pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL J. Bacteriol. 191:1480-1489(2009).
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; FM211187; CAR69229.1; -; Genomic_DNA.
DR RefSeq; WP_000164779.1; NC_011900.1.
DR AlphaFoldDB; B8ZL20; -.
DR SMR; B8ZL20; -.
DR KEGG; sne:SPN23F14390; -.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR PANTHER; PTHR30075; PTHR30075; 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..678
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197219"
SQ SEQUENCE 678 AA; 75439 MW; 8CFAEB8CFE5638EA CRC64;
MTKNLLVELG LEELPAYVVT PSEKQLGEKM AAFLKGKRLS FEAIQTFSTP RRLAVRVTGL
ADKQSDLTED FKGPAKKIAL DSDGNFTKAA QGFVRGKGLT VEDIEFREIK GEEYVYVTKE
EIGQAVEAIV PGIVDVLKSL TFPVSMHWAG NSFEYIRPVH TLTVLLDEQE FDLDFLDIKG
SRVSRGHRFL GQETKIQSAL SYEEDLRKQF VIADPCEREQ MIVDQIKEIE AKHGVRIEID
ADLLNEVLNL VEYPTAFMGS FDAKYLEVPE EVLVTSMKEH QRYFVVRDQD GKLLPNFISV
RNGNAERLKN VIKGNEKVLV ARLEDGEFFW REDQKLVISD LVEKLNNVTF HEKIGSLREH
MIRTGQITVL LAEKASLSVD ETVDLARAAA IYKFDLLTGM VGEFDELQGI MGEKYTLLAG
ETPAVAAAIR EHYMPTSAEG ELPESKVGAV LAIADKLDTI LSFFSVGLIP SGSNDPYALR
RATQGVVRIL DAFGWHIAMD ELIDSLYALK FDSLTYENKA EVMDFIKARV DKMMGSTPKD
IKEAVLAGSN FVVADMLEAA SALVEVSKEE DFKPSVESLS RAFNLAEKAE GVATVDSALF
ENDQEKALAE AVETLILSGP ASQQLKQLFA LSPVIDAFFE NTMVMAEDQA VRQNRLAILS
QLTKKAAKFA CFNQINTK