SYGB_LEUCK
ID SYGB_LEUCK Reviewed; 686 AA.
AC B1MZ60;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-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=LCK_00985;
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20;
RX PubMed=18281406; DOI=10.1128/jb.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(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; DQ489736; ACA82812.1; -; Genomic_DNA.
DR RefSeq; WP_004909367.1; NC_010471.1.
DR AlphaFoldDB; B1MZ60; -.
DR SMR; B1MZ60; -.
DR STRING; 349519.LCK_00985; -.
DR EnsemblBacteria; ACA82812; ACA82812; LCK_00985.
DR KEGG; lci:LCK_00985; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000002166; 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..686
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101297"
FT REGION 65..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 686 AA; 76496 MW; AC7C430F288946D6 CRC64;
MSTFLLEIGL EEVPAHLVTS SESQLVARTK EFLAAHRLTV GDIKPFSTPR RLALQLCDVA
EESEALSEEK RGPSVERAKD ENGEWSKAAQ GFARGQGATP EAFEERDGYV WLTKHTTGVP
ANQILSQIGE EVVSQMKFTT YMKWANHSFL YVRPIRWLVA LLDEQVINFN VLDIATGRVT
RGHRFLSTEH VTISDAQAYE ETLQSAYVLA DAENRKAQIK SQLETIANRN HWVLSLDNAP
AQDLLEEVNN IVEWPTAFSG SFDQKYLEVP DEVLITSMRE HQRFFYVRDT TGKLLPHFLS
VRNGDTAHLD NVIAGNEKVL VARLEDAEFF YREDQQKKIA DYMAKVKTLV FHEKIGTVYE
HMQRVGLLAE KLADALDFDD DKKTDLARAA EIYKFDLMTG MVGEFDELQG VMGEHYARLF
GENERVATAI REHYMPTSAN GNIAKSDVGA VLAIADKLDA IVTFFAANLI PSGSNDPYGL
RRAATGVVRT LTTKHWHIAL QPVLAEFMAA TGTVTASADL MAVLSFVVDR VRKLALDDDI
RQDIVSAGTD NFATADIVYL TDRIQVLANH AHDNNFREVI SALTRVARLA EKTPVSLNVN
PQLFENETEK ALYAATSELQ LVALEANGAE ALYQALAALQ MPISAYFDAT MVNVDNEQIK
NNRYAQLNII NQLIAGLGNL EDIVIK