ID E8X9L1_SALT4 Unreviewed; 505 AA.
AC E8X9L1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 01-MAY-2013, entry version 20.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
GN Name=lysS; OrderedLocusNames=STM474_3187;
OS Salmonella typhimurium (strain 4/74).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=909946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4/74;
RX PubMed=21478351; DOI=10.1128/JB.00394-11;
RA Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT "Genome sequences of Salmonella enterica serovar typhimurium,
RT Choleraesuis, Dublin, and Gallinarum strains of well- defined
RT virulence in food-producing animals.";
RL J. Bacteriol. 193:3162-3163(2011).
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 (By similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family.
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DR EMBL; CP002487; ADX18826.1; -; Genomic_DNA.
DR RefSeq; YP_005244025.1; NC_016857.1.
DR ProteinModelPortal; E8X9L1; -.
DR SMR; E8X9L1; 12-503.
DR PRIDE; E8X9L1; -.
DR EnsemblBacteria; ADX18826; ADX18826; STM474_3187.
DR GeneID; 11750717; -.
DR KEGG; seb:STM474_3187; -.
DR PATRIC; 47198066; VBISalEnt171491_3262.
DR KO; K04567; -.
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 Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1; -.
DR InterPro; IPR004364; aa-tRNA-synt_II.
DR InterPro; IPR018150; aa-tRNA-synt_II-like.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR002313; Lys-tRNA-ligase_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 PANTHER; PTHR22594; PTHR22594; 1.
DR PANTHER; PTHR22594:SF4; PTHR22594:SF4; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 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; Complete proteome; Cytoplasm;
KW Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT METAL 415 415 Magnesium 1 (By similarity).
FT METAL 422 422 Magnesium 1 (By similarity).
FT METAL 422 422 Magnesium 2 (By similarity).
SQ SEQUENCE 505 AA; 57575 MW; 48EBE562C708F96F CRC64;
MSEQNAQGAD EVVDLNNEMK ARREKLAALR EQGIPFPNDF RRDRTSDQLH AEFDAKEAEE
LEALNIEVSV AGRMMTRRIM GKASFVTLQD VGGRIQLYVA RDDLPEGVYN EQFKKWDLGD
ILGAKGKLFK TKTGELSIHC TELRLLTKAL RPLPDKFHGL QDQEARYRQR YLDLISNDES
RNTFKTRSKI LAGIRQFMVA RGFMEVETPM MQVIPGGASA RPFITHHNAL DLDMYLRIAP
ELYLKRLVVG GFERVFEINR NFRNEGISVR HNPEFTMMEL YMAYADYKDL IELTESLFRT
LAQDVLGTTQ VPYGDEVFDF GKPFEKLTMR EAIKKYRPET DMADLDNFDS AKAIAESIGI
HVEKSWGLGR IVTEIFDEVA EAHLIQPTFI TEYPAEVSPL ARRNDVNPEI TDRFEFFIGG
REIGNGFSEL NDAEDQAQRF LDQVNAKAAG DDEAMFYDED YVTALEHGLP PTAGLGIGID
RMVMLFTNSH TIRDVILFPA MRPVK
//
