ID   SYK_ACIAD               Reviewed;         509 AA.
AC   Q43990;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 151.
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=ACIAD1069;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9074511; DOI=10.1016/s0378-1119(96)00728-7;
RA   Geissdoerfer W., Ratajczak A., Hillen W.;
RT   "Nucleotide sequence of a putative periplasmic Mn superoxide dismutase from
RT   Acinetobacter calcoaceticus ADP1.";
RL   Gene 186:305-308(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; Z46863; CAA86924.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG67956.1; -; Genomic_DNA.
DR   RefSeq; WP_004921630.1; NC_005966.1.
DR   AlphaFoldDB; Q43990; -.
DR   SMR; Q43990; -.
DR   STRING; 62977.ACIAD1069; -.
DR   EnsemblBacteria; CAG67956; CAG67956; ACIAD1069.
DR   GeneID; 45233510; -.
DR   KEGG; aci:ACIAD1069; -.
DR   eggNOG; COG1190; Bacteria.
DR   HOGENOM; CLU_008255_6_0_6; -.
DR   OMA; EIFGEKC; -.
DR   OrthoDB; 63621at2; -.
DR   BioCyc; ASP62977:ACIAD_RS04925-MON; -.
DR   Proteomes; UP000000430; 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..509
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152592"
FT   BINDING         418
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         425
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         425
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   509 AA;  58079 MW;  95ED1AA43DC3D2F6 CRC64;
     MAQPNVQSTS EPILSENDLI AQRHAKLKQI QDKAKETGKS VWPNTFKREH YAADLQEQFK
     DIDKAQIEGS DKTYVKVAGR VMLNRGSFMV IQDMTGRIQL YVDRKGLPAD TLETIKSLDL
     GDIIAAEGYI GRSGKGDLYV HLEGFELLTK SLRPLPDKFH GLTDTEAKYR KRYLDLIVNE
     ETRKTFEIRA QVVAGIRAFL TNQRFMEVET PMMHVIPGGA SAQPFVTHHN ALDMELYLRI
     APELYLKRLV VGGFERVFEI NRNFRNEGVS TRHNPEFTMI EFYQAYADYK DLMQLTENML
     EKLALDILGT TDVPYGDEVY SFKGPFKKIS MFDAILEHNP DFTPENVNDR EFLAKFTQDV
     LKEQVKPGFG LGKLQTIVFE ETVETKLRQP TFITEYPAET SPLARRNDDN PHITDRFEFF
     IGGRELANGF SELNDPIDQA ERFQAQVAEK DAGDDEAMHY DADFIEALEY GLPPTAGQGI
     GIDRLVMIFA NAPSIRDVLL FPHMRRKDV