SYGB_LACJO
ID SYGB_LACJO Reviewed; 690 AA.
AC Q74IZ2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 122.
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=LJ_1319;
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533;
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS09139.1; -; Genomic_DNA.
DR RefSeq; WP_004897198.1; NC_005362.1.
DR AlphaFoldDB; Q74IZ2; -.
DR SMR; Q74IZ2; -.
DR STRING; 257314.LJ_1319; -.
DR PRIDE; Q74IZ2; -.
DR EnsemblBacteria; AAS09139; AAS09139; LJ_1319.
DR KEGG; ljo:LJ_1319; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000000581; 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; Reference proteome.
FT CHAIN 1..690
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006374"
SQ SEQUENCE 690 AA; 78024 MW; ECEA0F7EA388CA6A CRC64;
MTKDYLFEIG TEEMPAHVVS KSVKQLADRT KKYLKENGLS FKDIKTYSTP RRLTILVEDL
AEKQEDIDEV KKGPAKKIAQ DKDGNWTKAA QGFVRGQGMT TDDIYFEELK GTEYAYVHVQ
KEGKKASDIL MGMSDIVKAM TFPTKMRWGS YDFEFVRPIH WMVSLLGSEV VPVKLLDVVA
GRKTQGHRFL GDSVVLANAD DYEEALKSQY VIANADERKG MILNQIQELV AQHNWKVNID
KGLLEEVTNL VEYPTVFAGS FDEKYLNIPD EVLITSMKDN QRYFEVYDEN GKLINHFISV
RNGNSEYLDN VIAGNEKVLV ARLDDAQFFY DEDKKYPLAH FVDKLKNVSF HDKIGSVAEH
MARVQIIGDY LGKKFNVSDT EMKDFDRVSD IYKFDLVTSM VGEFAELQGV MGMHYARLIG
ENENVSVAIK ESYMPTSAEG DLPSTTVGSL LSIADKLDTI ISFFGAGMIP SSSNDPYALR
RNAYGIVRIL LNEGWSLPIK DVLPELIQLL SGKTAAKLPK DAEAENEIAD FIRDRVKQQL
QVEKYDYDVI DAVLASSQQD PIQILAAAKT LQMHHDDADF KPVVESLTRI TNILKKAKYR
NANDIDESLF QDVSEEELYA GVNALEENTD LSIADLYKGF VELQPVINNY FESNMILDKD
EKVKNNRLAQ LLKVNNLADR MGDLSKLVIK