ID   SYK_STAAU               Reviewed;         495 AA.
AC   Q53638;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Lysine--tRNA ligase;
DE            EC=6.1.1.6 {ECO:0000269|PubMed:12069408};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000303|PubMed:12069408};
DE            Short=LysRS;
GN   Name=lysS;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12600 / DSM 20231 / IAM 12544 / NCDO 949 / NCTC 8532;
RA   Green C.J., Vold B.S.;
RL   Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   CATALYTIC ACTIVITY.
RX   PubMed=12069408; DOI=10.1006/abio.2002.5700;
RA   Bonin P.D., Erickson L.A.;
RT   "Development of a fluorescence polarization assay for peptidyl-tRNA
RT   hydrolase.";
RL   Anal. Biochem. 306:8-16(2002).
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         Evidence={ECO:0000269|PubMed:12069408};
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; L36472; AAA53114.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53638; -.
DR   SMR; Q53638; -.
DR   PRIDE; Q53638; -.
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; IPR034762; Lys-tRNA-ligase_II_bac/euk.
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   PIRSF; PIRSF039101; LysRS2; 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; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..495
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152680"
FT   BINDING         406
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         413
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         413
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   495 AA;  56889 MW;  E5DC43EBCB0E9D98 CRC64;
     MSEEMNDQML VRRQKLQELY DLGIDPFGSK FDRSGLSSDL KEEWDQYSKE ELVEKEADSH
     VAIAGRLMTK RGKGKAGFAH VQDLAGQIQI YVRKDQVGDD EFDLWKNADL GDIVGVEGVM
     FKTNTGELSV KAKKFTLLTK SLRPLPDKFH GLQDIEQRYR QRYLDLITNE DSTRTFINRS
     KIIQEMRNYL NNKGFLEVET PMMHQIAGGA AARPFVTHHN ALDATLYMRI AIELHLKRLI
     VGGLEKVYEI GRVFRNEGVS TRHNPEFTMI ELYEAYADYH DIMDLTESMV RHIANEVLGS
     AKVQYNGETI DLESAWTRLH IVDAVKEATG VDFYEVKSDE ERKALAKEHG IEIKDTMKYG
     HILNEFFEQK VEETLIQPTF IYGHPTEISP LAKKNPEDPR FTDRFELFIV GREHANRFTE
     LNDPIDQKGR FEAQLVEKAQ GNDEAHEMDE DYIEALEYGM PPTGGLGIGI DRLVMLLTDS
     PSIRDVLLFP YMRQK