ID   SYGB_STRS2              Reviewed;         678 AA.
AC   A4W3J4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=SSU98_1775;
OS   Streptococcus suis (strain 98HAH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98HAH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(2007).
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; CP000408; ABP92933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4W3J4; -.
DR   SMR; A4W3J4; -.
DR   KEGG; ssv:SSU98_1775; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
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..678
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101358"
SQ   SEQUENCE   678 AA;  75263 MW;  10513561BDEE2AD4 CRC64;
     MTKNLLVELG LEEIPAYIVT PAMHQLRDRM ATFLTDNRLA FDSIDVFSTP RRLAVRVRGL
     ADQQTDLTED FKGPAKKIAL DADGNFTKAA EGFVRGKGLT TADIEFREIK GEEYVYVTKH
     EAGQPAKTVL AGIPEVLKAM TFPVSMNWAS NKFAYIRPVH TLTVLLDDEA LDMDFLDITS
     GRISRGHRFL GNETEIASAD SYEADLRAQF VITDPAERQN MIVEQIKAIE DKHNVTVEID
     EDLLNEVLNL VEYPTAFMGS FDTKYLEVPE EVLVTSMKNH QRYFVVRDKA GKLLPNFISV
     RNGNDQYLDN VIKGNEKVLV ARLEDGEFFW REDQKLKIAD LVERLKVVTF HEKIGSLYEH
     MERTKVIAEK LADLAGLSAG EKADVARAAD IYKFDLLTGM VGEFDELQGI MGEKYALLAG
     EKPAVAAAIR EHYLPNSAEG ELPESKVGAV LALADKFDTL LSFFSVGLIP SGSNDPYALR
     RATQGIVRIL EAFGWEIPLD QLIAELYSLN FASLTYDNQP AVMDFIRARV EKMMDKTIPK
     DIREAVLASS TFVVRLQLAA SSAIFQKAKE ADYKEAVENL SRVFNLAEKA EVTAIDEALF
     ENDQEKALAA AVAGLELTED MAGNLDKLFA LSPVIAAFFD NTMVMVDDAT VKANRLALLK
     ALADKASAVA VFNLLNSK