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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
 
 
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