SYGB_LACH4
ID SYGB_LACH4 Reviewed; 687 AA.
AC A8YVM4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=lhv_1298;
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571;
RX PubMed=17993529; DOI=10.1128/jb.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(2008).
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; CP000517; ABX27311.1; -; Genomic_DNA.
DR RefSeq; WP_003628907.1; NC_010080.1.
DR AlphaFoldDB; A8YVM4; -.
DR SMR; A8YVM4; -.
DR STRING; 405566.lhv_1298; -.
DR PRIDE; A8YVM4; -.
DR EnsemblBacteria; ABX27311; ABX27311; lhv_1298.
DR KEGG; lhe:lhv_1298; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000000790; 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.
FT CHAIN 1..687
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000071879"
SQ SEQUENCE 687 AA; 78504 MW; 5986D58CF160923F CRC64;
MAKDYLFEIG TEEIPAHVVP RSVKQLADRT RKFLKENGLK FKDIKTFSTP RRLTILVEDL
AEKQDDIDEV KKGPAKKITQ DADGNWTKAA QGFARGQGMT TDDIYFEELK GTEYAYVHVQ
KEGKKASDIL LGMSDIIKAM TFPTKMRWDS NDFEFVRPIH WLVSLFGSDV IPVKILDITA
GRKTQGHRFL GDSVVLANAD DYEDALKDQY VIANAEERKD MIVNQMNELV KKNHWQIKPD
RDLLEEVTYL VEYPTVFAGS FDEKYLNIPD EVLITSMKDN QRYFEVYDEN GKLINHFIAV
RNGNKDYLDN IISGNEKVLV ARLDDAQFFY DEDRKYPLSH FVDRLKNVSF HDKIGSMAEK
IQRVRMIGDY LAKRWDLPEN VVTDFDRASE LYKFDLVTQM VGEFAELQGV MGMHYARLAG
EDEEVSVAIK EHYMPATAEG PLPETTVGSL LSVADKIDTI ITFFGAGMIP TSSNDPYALR
RYAYGIVRIL LNEKWSLPFN EVLPEIINML GGVTPAKLPK GDSEQEIADF IRDRVKQYLQ
KNKFKYDIVD AVLASSQQDP SQILAAANVL QLHHDDEEFK PVVESLTRIN NILKKAKFNG
KVDVDESLFV DNSETELYAR VQNLQNIESL ADLYQGFVHL QPVIDQYFEA NMIMDKDENV
KNNRLAQLYA VSELADRLGD LSKLVIK