SYGB_STRPI
ID SYGB_STRPI Reviewed; 678 AA.
AC B1ICQ5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=SPH_1590;
OS Streptococcus pneumoniae (strain Hungary19A-6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=487214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hungary19A-6;
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000936; ACA35991.1; -; Genomic_DNA.
DR RefSeq; WP_000164769.1; NC_010380.1.
DR AlphaFoldDB; B1ICQ5; -.
DR SMR; B1ICQ5; -.
DR PRIDE; B1ICQ5; -.
DR EnsemblBacteria; ACA35991; ACA35991; SPH_1590.
DR GeneID; 66806574; -.
DR KEGG; spv:SPH_1590; -.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000002163; Chromosome.
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_1000101354"
SQ SEQUENCE 678 AA; 75471 MW; E0BA828747383B5C CRC64;
MTKNLLVELG LEELPAYVVT PSEKQLGEKM AAFLKENRLS FEAIQTFSTP RRLAVRVTGL
SDKQSDLTED FKGPAKKIAL DSDGNFTKAA QGFVRGKGLT VEDIEFREIK GEEYVYVTKE
EVGQSVEAIV PGVVDVLKSL TFPVSMHWAG NSFEYIRPVH TLTVLLDEQE FDLDFLDIKG
SRVSRGHRFL GKETKIQSAL SYEEDLRKQF VIADPCEREQ MIVDQIKEIE AKHGVRIEID
ADLLNEVLNL VEYPTAFMGS FDAKYLEVPE EVLVTSMKEH QRYFVVRDQD GKLLPNFISV
RNGNAERLKN VIKGNEKVLV ARLEDGEFFW REDQKLVISD LVEKLNNVTF HEKIGSLREH
MIRTGQITVL LAEKAGLSVD 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