SYK_MYCLE
ID SYK_MYCLE Reviewed; 507 AA.
AC P46861;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
DE Short=LysRS;
GN Name=lysS; OrderedLocusNames=ML0233;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 449-507.
RX PubMed=1840579; DOI=10.1128/iai.59.11.4117-4124.1991;
RA Sela S., Thole J.E., Ottenhoff T.H., Clark-Curtiss J.E.;
RT "Identification of Mycobacterium leprae antigens from a cosmid library:
RT characterization of a 15-kilodalton antigen that is recognized by both the
RT humoral and cellular immune systems in leprosy patients.";
RL Infect. Immun. 59:4117-4124(1991).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AL583917; CAC29741.1; -; Genomic_DNA.
DR EMBL; M67510; AAA25350.1; -; Genomic_DNA.
DR PIR; A43601; A43601.
DR PIR; A86938; A86938.
DR RefSeq; NP_301293.1; NC_002677.1.
DR RefSeq; WP_010907617.1; NC_002677.1.
DR AlphaFoldDB; P46861; -.
DR SMR; P46861; -.
DR STRING; 272631.ML0233; -.
DR EnsemblBacteria; CAC29741; CAC29741; CAC29741.
DR KEGG; mle:ML0233; -.
DR PATRIC; fig|272631.5.peg.366; -.
DR Leproma; ML0233; -.
DR eggNOG; COG1190; Bacteria.
DR HOGENOM; CLU_008255_6_0_11; -.
DR OMA; EIFGEKC; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd04322; LysRS_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002313; Lys-tRNA-ligase_II.
DR InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00499; lysS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..507
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152649"
FT BINDING 417
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 507 AA; 56421 MW; 52BF33D6287C96B3 CRC64;
MNADPLETDA ALPEQFRIRR DKRARLLAEG RDPYPVAIER THTLAEVRAA YPDLATDSAT
DDIVGIAGRV IFARNSGKLC FATLQDGDGT NLQVMISLNK VGSETLDAWK VDVDLGDIVY
VHGNVISSRS GELSVLADSW QMVSKSLRPL PVAHKEMSEE SRVRQRYVDL IVCPQVRIVA
HQRIAVIRAI RTALERRGFL EVETPMLQTL AGGAAARPFV THSNALDIDL YLRIAPELFL
KRCIVGGFDK VFELNRVFRN EGADSTHSPE FSMLETYQTY GTYDDSAVVT REIIQEVADE
AIGTRQLQMP DDSVYDIDGE WETIQMYPSL SAVLGEEITP QTSVDRLRAI ADRLGRGIGP
EILDKPSYGH GRLVEQLWEY TVGNTLSAPT FVKDFPVETT PLTRQHRSIP GVTEKWDLYL
RGVELATGYS ELNDPVVQRE RFGQQVRAAA AEEDEAMALD EEFLAALEYA MPPCTGTGMG
IDRLLMSLTG LSIRETVLFP IVRPHSN
