ID   SYGB_STRA5              Reviewed;         679 AA.
AC   Q8E1T3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=SAG0270;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(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; AE009948; AAM99177.1; -; Genomic_DNA.
DR   RefSeq; NP_687305.1; NC_004116.1.
DR   RefSeq; WP_000159081.1; NC_004116.1.
DR   AlphaFoldDB; Q8E1T3; -.
DR   SMR; Q8E1T3; -.
DR   STRING; 208435.SAG0270; -.
DR   EnsemblBacteria; AAM99177; AAM99177; SAG0270.
DR   KEGG; sag:SAG0270; -.
DR   PATRIC; fig|208435.3.peg.268; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000821; Chromosome.
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; Reference proteome.
FT   CHAIN           1..679
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101345"
SQ   SEQUENCE   679 AA;  76530 MW;  85E63448B4FCD9C9 CRC64;
     MTKDLLLELG LEELPAYVVT PSEKQLGQKM VKFLEDHRLS FETVQIFSTP 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 KMKQNRLAIL
     NSLVAKARTV AAFNLLNTK