SYGB_STRSY
ID SYGB_STRSY Reviewed; 678 AA.
AC A4VX91;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=SSU05_1764;
OS Streptococcus suis (strain 05ZYH33).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=391295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05ZYH33;
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; CP000407; ABP90730.1; -; Genomic_DNA.
DR AlphaFoldDB; A4VX91; -.
DR SMR; A4VX91; -.
DR STRING; 391295.SSU05_1764; -.
DR EnsemblBacteria; ABP90730; ABP90730; SSU05_1764.
DR KEGG; ssu:SSU05_1764; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000000243; 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..678
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101360"
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