SYGB_STRTD
ID SYGB_STRTD Reviewed; 678 AA.
AC Q03LV6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=STER_0540;
OS Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=322159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-491 / LMD-9;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000419; ABJ65816.1; -; Genomic_DNA.
DR RefSeq; WP_011680845.1; NC_008532.1.
DR AlphaFoldDB; Q03LV6; -.
DR SMR; Q03LV6; -.
DR KEGG; ste:STER_0540; -.
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_1000101361"
SQ SEQUENCE 678 AA; 74442 MW; 1EB2A9B0CFF03FCB CRC64;
MTKNLLVELG LEELPAYVVT PSEKQLGEKM AAFLGENRLS YESIQTFSTP RRLAVRVLGL
ADQQTDLTED FKGPSKKIAL DADGNFSKAA QGFVRGKGLT VDDIEFREVK GEEYVYVTKH
EAGKSAKEVL AGIPEVLASL TFPVSMHWAN NSFEYIRPVH TLIVLLGDEA LELDFLGIKS
GRVSRGHRFL GHEVEITNAD SYEEDLRTVY VIADSKEREN MIREQIKAIE AEQGVQVQIE
EGLLNEVLNL VEYPTTFMGG FDTKYLDVPE DVLVTSMETH QRYFVVRDLD GRLKPNFISV
RNGNAEHLEN VVRGNEKVLV ARLEDGEFFW REDQKLKIED LVAKLANVTF HEKIGSLSEH
MARAGVIAAS LAEKAGLTAE EKAAVARAAE IYKFDLLTGM VGEFDELQGI MGEKYALLAG
EDEAVATAIR EHYLPDSADG ALPETKVGAI LALADKLDTL LSFFSVGLIP SGSNDPYALR
RATQGIVRIL DAFGWHIPMD ELIDSLYGLS FDSLSYDNQA EVIRFIKARV DKMMGSTPKD
IKEAVLSGSN FVVADMLEAA EALSEAAKTD GYKAAVESLS RAFNLAEKAD TSVAVDASLF
ENDQEKALAQ VAESLELTGS ASDKLAQLFV LSPVIDAFFD NTMVMADDVA VKNNRLALLS
ALVAKAKTVA AFNQLNTK