ID   SYK_THETH               Reviewed;         492 AA.
AC   P41255;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Lysine--tRNA ligase;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysyl-tRNA synthetase;
DE            Short=LysRS;
GN   Name=lysS;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-28.
RC   STRAIN=VK1;
RX   PubMed=8169220; DOI=10.1128/jb.176.9.2699-2705.1994;
RA   Chen J., Brevet A., Lapadat-Tapolsky M., Blanquet S., Plateau P.;
RT   "Properties of the lysyl-tRNA synthetase gene and product from the extreme
RT   thermophile Thermus thermophilus.";
RL   J. Bacteriol. 176:2699-2705(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
RX   PubMed=8947055; DOI=10.1002/j.1460-2075.1996.tb01022.x;
RA   Cusack S., Yaremchuk A., Tukalo M.;
RT   "The crystal structures of T. thermophilus lysyl-tRNA synthetase complexed
RT   with E. coli tRNA(Lys) and a T. thermophilus tRNA(Lys) transcript:
RT   anticodon recognition and conformational changes upon binding of a lysyl-
RT   adenylate analogue.";
RL   EMBO J. 15:6321-6334(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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; X70708; CAA50039.1; -; Genomic_DNA.
DR   RefSeq; WP_011173121.1; NZ_CP053287.1.
DR   AlphaFoldDB; P41255; -.
DR   SMR; P41255; -.
DR   GeneID; 3170107; -.
DR   OMA; EIFGEKC; -.
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   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..492
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152697"
FT   BINDING         395
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         402
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         402
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   492 AA;  56921 MW;  DFF340D4BC06CCA5 CRC64;
     MNDQTRQRLL NLEALVEAGF APYPYRFPKT HSAEAILKAK RGAPPESEWP EEEVAVAGRL
     VALRRMGKVT FAHLLDETGR IQLYFQRDLT PKYELLKKLD VGDILGVRGH PFTTKTGEVT
     VKVLDWTPLV KSLHPLPDKW HGLRDKEVRY RQRYLDLIVN PEVREVFRRR SEIVRYIRRF
     FEAKGFLEVE TPILQPTTGG AEARPFKTYH NALDHEFYLR ISLELYLKRL LVGGYEKVFE
     IGRNFRNEGI DHNHNPEFTM LEAYWAYADY QDMAGLVEEL LSGLVLHLFG SHEVPYQGRV
     LNFKPPFRRI SFVEALKEKA GLPFDPLDLE RLRLWADAHH PELSQVPNYK LLDKLFGIYV
     EPELQDPTFV FDFPLAISPL AKRHREKPGL VERWDLYAGG MELAPCYSEL NDPLDQRERF
     LEQARRRKEG DEEAPEPDED FLLALEYGMP PAAGLGLGID RLAMLLTDQP SLRDVLLFPL
     LKPKKEAVEE GV