ID   SYGB_STRA1              Reviewed;         679 AA.
AC   Q3K3A9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=SAK_0342;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA   Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA   Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA   Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA   Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA   Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA   Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA   Wessels M.R., Rappuoli R., Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
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; CP000114; ABA44827.1; -; Genomic_DNA.
DR   RefSeq; WP_000159101.1; NC_007432.1.
DR   AlphaFoldDB; Q3K3A9; -.
DR   SMR; Q3K3A9; -.
DR   KEGG; sak:SAK_0342; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 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_1000101343"
SQ   SEQUENCE   679 AA;  76518 MW;  1327D973B9B769CC CRC64;
     MTKDLLLELG LEELPAYVVT PSEKQLGQKM VKFLEDHRLS FETVQTFSTP RRLAVRVKGL
     ADQQTDLTED FKGPSKKIAL DAEGNFSKAA QGFVRGKGLS VDDIEFREVK GEEYVYVTKH
     ETGKSAIDVL ASVTEVLTEL TFPVNMHWAN NSFEYIRPVH TLVVLLDDQA LELDFLDIHS
     GRISRGHRFL GSDTEISSAS SYEDDLRQQF VIADAKERQQ MIVNQIHAIE EKKNISVEID
     EDLLNEVLNL VEYPTAFLGS FDEKYLDVPE EVLVTSMKNH QRYFVVRDRD GKLLPNFISV
     RNGNAEHIEN VIKGNEKVLV ARLEDGEFFW QEDQKLNIAD LVEKLKQVTF HEKIGSLYEH
     MDRVKVISQY LAEKADLSDE EKLAVLRAAS IYKFDLLTGM VDEFDELQGI MGEKYALLAG
     EQPAVAAAIR EHYMPTSADG ELPETRVGAI LALADKFDTL LSFFSVGLIP SGSNDPYALR
     RATQGIVRIL EAFGWDIPLD ELVTNLYGLS FASLDYANQK EVMAFISARI EKMIGSKVPK
     DIREAVLESD TYIVSLILEA SQALVQKSKD AQYKVSVESL SRAFNLAEKV THSVLVDSSL
     FENNQEKALY QAILSLELTE DMHDNLDKLF ALSPIINDFF DNTMVMTDDE KMKQNRLALL
     NSLVAKARTV AAFNLLNTK