SYGB_STRP3
ID SYGB_STRP3 Reviewed; 679 AA.
AC P0DG38; Q879I0; Q8K663;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 49.
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=SpyM3_1471;
OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=198466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-595 / MGAS315;
RX PubMed=12122206; DOI=10.1073/pnas.152298499;
RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT encoded toxins, the high-virulence phenotype, and clone emergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM80078.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014074; AAM80078.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011054911.1; NC_004070.1.
DR AlphaFoldDB; P0DG38; -.
DR SMR; P0DG38; -.
DR EnsemblBacteria; AAM80078; AAM80078; SpyM3_1471.
DR KEGG; spg:SpyM3_1471; -.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000000564; 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..679
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000072930"
SQ SEQUENCE 679 AA; 74996 MW; 4790D9F956022D50 CRC64;
MSKNLLIELG LEELPAYVVT PSEKQLGERL ATFLTENRLS FEDIQTFSTP RRLAVRVSGL
AAQQTDLTED FKGPAKKIAL DADGNFSKAA QGFVRGKGLT TDAIEFREVK GEEYVYVTKH
EAGKPAKEVL LGVTEVLSAM TFPVSMHWAN NSFEYIRPVH TLTVLLNDEA LELDFLDIHS
GRVSRGHRFL GTETTITSAD SYEADLRSQF VIADAKERQE MIVEQIKAIE AAQGVQVDID
ADLLNEVLNL VEFPTAFMGS FDAKYLDVPE EVLVTSMKNH QRYFVVRDQE GHLMPNFVSV
RNGNDQAIEN VIKGNEKVLV ARLEDGEFFW REDQKLQIAD LVAKLTNVTF HEKIGSLAEH
MDRTRVIAAS LAKEANLSAE EVTAVDRAAQ IYKFDLLTGM VGEFDELQGI MGEKYARLAG
EDAAVATAIR EHYLPDAAGG ALPETKVGAV LALADKLDTL LSFFSVGLIP SGSNDPYALR
RATQGIVRIL DHFGWRIPMD KLVDSLYDLS FDSLTYANKA DVMNFIRARV DKMMGKAVPK
DIREAVLESS TFVVPEMLAA AEALVKASHT ENYKPAVESL SRAFNLAEKA DASVHVDPSL
FENEQENTLF AAIQGLTLAG SAAQQLEQVF VLSPVINDFF DNTMVMAEDQ ALKNNRLAIL
SDLVSKAKTI AAFNQLNTK