ID   SYGB_STRMU              Reviewed;         679 AA.
AC   Q8CWY5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=SMU_446;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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; AE014133; AAN58196.1; -; Genomic_DNA.
DR   RefSeq; NP_720890.1; NC_004350.2.
DR   RefSeq; WP_002262082.1; NC_004350.2.
DR   AlphaFoldDB; Q8CWY5; -.
DR   SMR; Q8CWY5; -.
DR   STRING; 210007.SMU_446; -.
DR   PRIDE; Q8CWY5; -.
DR   EnsemblBacteria; AAN58196; AAN58196; SMU_446.
DR   KEGG; smu:SMU_446; -.
DR   PATRIC; fig|210007.7.peg.392; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   PhylomeDB; Q8CWY5; -.
DR   Proteomes; UP000002512; 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; Reference proteome.
FT   CHAIN           1..679
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101347"
SQ   SEQUENCE   679 AA;  77121 MW;  810470A8C8D865C6 CRC64;
     MTKNLLVELG LEEMPAYVVK PSIKQLRQKM GQFLETNRLS FEKIEMFSTP RRLAIRVVHL
     ADQQSDYSED FKGPAKKIAL DADGHFTKAA QGFVRGKGLT TDAIEFREVK GEEYVYVTKN
     EAGKPAKEVL GGLIDVLQSL TFPVNMHWAN HTFEYIRPVH TLVVLLDDEA LDLNFLDIKS
     GRISRGHRFL GQETQIASAA SYETDLRAEF VIADAKERED MIIEQIREIE KTYNVSVEID
     EALLSEVLNL VEYPTAFMGS FDEKYLELPE EVLVTSMKTH QRYFVVRDQT GKLLPNFISV
     RNGNEQFIEN VVKGNEKVLL ARLEDGEFFW REDQRLQIAD LVEKLKLVTF HEKIGSLYEH
     MMRTKQIAAY LAEQADLTDQ EKAEIERAAS IYKFDLLTGM VGEFDELQGI MGEKYATLAG
     ESQAVATAVR EHYLPISSDG QLPDSKVGAI LAVADKLDTL LSFFSVGLIP SGSNDPYALR
     RATQGIVRIL DKFGWEIPLD RLVANLYQFD FDSLTYQNQA DVLAFIRGRV EKMIDKSVPK
     DIREAVLDSS THIVRLEVEA AAALAEKADE DHFKASIESL SRVFNLAEKS NHNEMVDTSI
     FENEYEQELF DAVEELHFTE DMTDNVDRLF VLSPIIDAFF DNTMVMVDDE AVKKNRLNLL
     DRLAQKANTI AAFNEIRTK