SYGB_LIGS1
ID SYGB_LIGS1 Reviewed; 693 AA.
AC Q1WTP1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=LSL_0911;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(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; CP000233; ABD99721.1; -; Genomic_DNA.
DR RefSeq; WP_011476035.1; NC_007929.1.
DR RefSeq; YP_535804.1; NC_007929.1.
DR AlphaFoldDB; Q1WTP1; -.
DR SMR; Q1WTP1; -.
DR STRING; 362948.LSL_0911; -.
DR EnsemblBacteria; ABD99721; ABD99721; LSL_0911.
DR KEGG; lsl:LSL_0911; -.
DR PATRIC; fig|362948.14.peg.988; -.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000006559; 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..693
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006375"
SQ SEQUENCE 693 AA; 78206 MW; CD7E92D3B49F3F8D CRC64;
MAHTFLLEIG LEEIPAHVVT PSVNQLVQKT TKFLKEQRID FDEVIPYSTP RRLTVKVTGL
ADKQADIEEE AKGPSKKIAL DDEGNWSKAA QGFVRGQGVT VDDIFFKELK GTEYVYVKKF
IPGKPVSEVL TGMKDVAMDL KFPTMMRWGS NDFEYVRPIK WLVALLDDEV VPFEILDIKT
GRTTQGHRFL GEAVDVPSAD KYLETLETQK VIADAGVRKA EIRKQIDDLA TENNWNIVVD
EDLLEEVNNL VEYPTVFAGK FKEEYLQVPN EVLITSMKDH QRFFYVTDKD GNLLPNFVSV
RNGNKDYLEN VVAGNEKVLT ARLEDAKFFY EEDQQHTIAD YVERLKKVMF HDKIGTIYEK
MERVNLLAKF LGNKLGLSET ELKDLDRASM IYKFDLVTGM VGEFSELQGI MGEIYARLQG
EDDNVSTAIR EEYMPTSSEG ELPQSNVGAV LSIADKLDSI QSFFAANMIP SGSNDPYALR
RQALGIIRIA LDKGWDISLP LLHEAINYAY AEREDLYKNT QPITNVSETD SFVIDRLAQV
LSGNKFRRDI LDAVVARADM PFIQALQAAQ VLSKHAEDDN FKEVIEALTR VTRLAKKAPE
FGSDAVIDST LFENDTEKVL ADEFAKVEAG YGDAEMNEKF TILSSLKDSI TAYFDATMIM
ADDEKVKNNR LLQLVKIAEL TEDFGSLDKL IVK