SYGB_LACLM
ID SYGB_LACLM Reviewed; 673 AA.
AC A2RL88;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=llmg_1477;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(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; AM406671; CAL98055.1; -; Genomic_DNA.
DR RefSeq; WP_011835326.1; NZ_WJVF01000002.1.
DR AlphaFoldDB; A2RL88; -.
DR SMR; A2RL88; -.
DR STRING; 416870.llmg_1477; -.
DR EnsemblBacteria; CAL98055; CAL98055; llmg_1477.
DR KEGG; llm:llmg_1477; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR PhylomeDB; A2RL88; -.
DR BioCyc; LLAC416870:LLMG_RS07450-MON; -.
DR Proteomes; UP000000364; 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.
FT CHAIN 1..673
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101293"
SQ SEQUENCE 673 AA; 75642 MW; F85E2D9218E5DE13 CRC64;
MTNYLLEIGL EEIPAHLVTP SINQLAERME AFLNENRLKF DKIIKFSTPR RLALIVEELS
DSSEAIDEEV KGPSAKIAKD AEGNWSKAIQ GFSRGQGATP DDLILKGDYY YAKKHVDGVK
SEEILSKVGD EVIAKMTFST YMKWGNNDFL FVRPIQWIVS LLEDEIVAFD LLDVTANRFS
RGHRFLANVE IELKNANDYA SKMPENFVLV DAEHRKAEIS AQILALASEN NWQVTLHKDL
LEEVNNIVEY PTAFVGSFDP KYLSVPAEVL VTSMRDNQRY FEVYNQEGQL APNFISVRNG
NAEHIENVVL GNEKVLFARL EDAEFFWKED QKLKIEDLVA KLAKVTFHAK IGSITEHMAR
TKLIAAKLAD IAGLTDEEKV DVARSAEIYK FDLLTGMVGE FDELQGVMGE KYALLAGENA
NVAAAIREHY MPTSADGQLP ETKVGSVLAA ADKIDSVLSF FNVGLIPSGS NDPYALRRAV
QGLIRIIEKM NWHFDLSLFI DQFEGQNHAE ILEFVKARVQ KLLLEKLDRY DIVEAAINSS
NFDITNMMES AFVIDGHKLH EPFKPAIENV SRSINLVKKA ADIAEINPAL FEEDTEQALY
DAVISLQNQW TYKPCEEKFR AIVHMLAPAI EAFFDNVMVM AEDLAVRDNR IALLSEVVAL
TSVMADFSLI NTK