SYK_MYCPN
ID SYK_MYCPN Reviewed; 489 AA.
AC P75500;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=MPN_277; ORFNames=MP558;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96206.1; -; Genomic_DNA.
DR PIR; S73884; S73884.
DR RefSeq; NP_109965.1; NC_000912.1.
DR RefSeq; WP_010874634.1; NC_000912.1.
DR AlphaFoldDB; P75500; -.
DR SMR; P75500; -.
DR IntAct; P75500; 2.
DR STRING; 272634.MPN_277; -.
DR PRIDE; P75500; -.
DR EnsemblBacteria; AAB96206; AAB96206; MPN_277.
DR GeneID; 66609074; -.
DR KEGG; mpn:MPN_277; -.
DR PATRIC; fig|272634.6.peg.297; -.
DR HOGENOM; CLU_008255_6_0_14; -.
DR OMA; EIFGEKC; -.
DR BioCyc; MPNE272634:G1GJ3-435-MON; -.
DR Proteomes; UP000000808; 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; cd00775; LysRS_core; 1.
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..489
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152651"
FT BINDING 399
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 489 AA; 56081 MW; E3D643B73DEDBCA0 CRC64;
MSDRLNDQAQ NRLQKLLNLK QTGNDPYLIT KIENTHSAAS FQKAFANQSD AELKQYQVIL
TGRIIALRQT FIIIQDFSGK MQLYINKKTA PELFEYFNNY IDLGDQIVAT GHPMMTKTGV
LTLNVERLQI VAKCLQTPPE KWHGLTDPEA RARKRYLDLT YNRAQVEVFL KRTQIITAIR
TFLNEAGFLE VETPILQAVL GGANAKPFKT HYNALKGDFY LRIANEIALK KLIVGGLPKV
YEMGRMFRNE GVDTTHNPEF TSIEMYQANA DYAVMMDLTE NLIKFVCKTL NQWSFNWNGQ
TLDLAKPFKK VKMVDLICQV TGVNFDDVKD DQTAIALAKQ HKVELKKHEQ NKQHIINRFF
EQFCEHTLIQ PTFVTHYPKA VSPLAKQDPH NPEFTERFEL FINTKELANA YSELNDPLEQ
RARFEQQLQE KRMGNDEASE LDESFLDALS FGLPPTGGLG IGVDRLVMLL CECSSIRDVV
FFPQLRELK
