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   16-JUN-2009, entry version 68.
DE   RecName: Full=Lysyl-tRNA synthetase;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysine--tRNA ligase;
DE            Short=LysRS;
GN   Name=lysS; OrderedLocusNames=ACIAD1069;
OS   Acinetobacter sp. (strain ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=97228433; 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
RT   from Acinetobacter calcoaceticus ADP1.";
RL   Gene 186:305-308(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate
CC       + L-lysyl-tRNA(Lys).
CC   -!- COFACTOR: Binds 3 magnesium ions per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; Z46863; CAA86924.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG67956.1; -; Genomic_DNA.
DR   RefSeq; YP_045778.1; -.
DR   HSSP; P13030; 1BBW.
DR   GeneID; 2878610; -.
DR   GenomeReviews; CR543861_GR; ACIAD1069.
DR   KEGG; aci:ACIAD1069; -.
DR   NMPDR; fig|62977.3.peg.1217; -.
DR   HOGENOM; Q43990; -.
DR   OMA; Q43990; ANEESRH.
DR   BioCyc; ASP62977:ACIAD1069-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00252; -; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR002313; Lys-tRNA-synth_II.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA_bd_OB_tRNA-helicase.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   PANTHER; PTHR22594:SF4; tRNA-synt_lys_2; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
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; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    509       Lysyl-tRNA synthetase.
FT                                /FTId=PRO_0000152592.
FT   METAL       418    418       Magnesium 1 (By similarity).
FT   METAL       425    425       Magnesium 1 (By similarity).
FT   METAL       425    425       Magnesium 2 (By similarity).
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
//