ID   SYK_LEPBJ               Reviewed;         495 AA.
AC   Q04SM4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00252};
DE            EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00252};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00252};
DE            Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00252};
GN   Name=lysS {ECO:0000255|HAMAP-Rule:MF_00252}; OrderedLocusNames=LBJ_1523;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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:0000255|HAMAP-Rule:MF_00252};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00252};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00252};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00252}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00252}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00252}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000350; ABJ76096.1; -; Genomic_DNA.
DR   RefSeq; WP_011670315.1; NC_008510.1.
DR   AlphaFoldDB; Q04SM4; -.
DR   SMR; Q04SM4; -.
DR   EnsemblBacteria; ABJ76096; ABJ76096; LBJ_1523.
DR   KEGG; lbj:LBJ_1523; -.
DR   HOGENOM; CLU_008255_6_0_12; -.
DR   OMA; EIFGEKC; -.
DR   Proteomes; UP000000656; Chromosome 1.
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.
FT   CHAIN           1..495
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_1000012886"
FT   BINDING         406
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT   BINDING         413
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT   BINDING         413
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
SQ   SEQUENCE   495 AA;  56621 MW;  DD107215CB518DC3 CRC64;
     MLDSNELIQQ RIQKIEDLKN QGINPYPVRF FPDSKSKDIV EKFEKDPTGP ETKFKLGGRL
     HSKRVMGKAS FAHLKDSTGI IQLYATRDDL GEISYSIFKS LDLGDIIGLE GYLFKTQKGE
     VTLHVTSVEL LAKCIRPLPV VKEKDGVIYD AFADVEQRYR MRYVDLVVND HVRDTFITRS
     RIVSEIRNFL TNEGFLEVET PMMQPIAGGA AARPFVTHHN TLDMQLFLRI APELYLKRLI
     VGGMDRVFEL NRNFRNEGIS TKHNPEFTMM EAYIAFADMN TMLDLTERLI THLAQKIHGA
     LKIQYGKDLI DLSPPWRKIT YTDIIKEYSG IDFSLITSLE EAKKKASELN VDVSKCNTIW
     KVADEVFSEK AEPNLIQPVF IIDYPKELSP LAKSNPDKPG YVERFEPYVA GREIGNAFTE
     LNDPFDQKER FEDQVQQREA GDDEAFMMDE DYIRALEYGM PPTGGLGIGI DRLVMLLTDS
     HSIRDTILFP LMRPE