Lysyl-tRNA synthetase, heat inducible (P0A8N5)

Identification
Name:Lysyl-tRNA synthetase, heat inducible
Synonyms:
  • Lysine--tRNA ligase
  • LysRS
Gene Name:lysU
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Also can synthesize a number of adenyl dinucleotides (in particular AppppA). These dinucleotides have been proposed to act as modulators of the heat-shock response and stress response
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Lys)+1.0tRNA(Lys) ↔ 1.0Thumb+1.0Thumb+1.0L-Lysyl-tRNA+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Lysine + 1.0tRNA(Lys) + 1.0tRNA(Lys) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Lysyl-tRNA + 1.0L-Lysyl-tRNA
ReactionCard
SMPDB Reactions:
1.0L-Lysine+1.0Thumb+1.0Thumb+1.0tRNA(Lys)+1.0Thumb → 1.0Thumb+1.0Pyrophosphate+1.0L-Lysyl-tRNA
1.0L-Lysine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Lys) + 1.0L-Lysine → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Lysyl-tRNA
ReactionCard
EcoCyc Reactions:
2.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
2.0Adenosine triphosphate + 1.0Hydrogen ion → 1.0Diadenosine tetraphosphate + 1.0Pyrophosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Lys) → 1.0Thumb+1.0L-Lysine-tRNA (Lys)+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Lysine + 1.0tRNA(Lys) → 1.0Adenosine monophosphate + 1.0L-Lysine-tRNA (Lys) + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01211Diadenosine tetraphosphateMetaboCard
ECMDB21431Diadenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00182L-LysineMetaboCard
ECMDB23777L-Lysyl-tRNAMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
aminoacyl-tRNA ligase activity
ATP binding
binding
catalytic activity
ligase activity
ligase activity, forming aminoacyl-tRNA and related compounds
ligase activity, forming carbon-oxygen bonds
lysine-tRNA ligase activity
nucleic acid binding
nucleoside binding
nucleotide binding
purine nucleoside binding
Process
biosynthetic process
cellular macromolecule biosynthetic process
cellular macromolecule metabolic process
lysyl-tRNA aminoacylation
macromolecule biosynthetic process
macromolecule metabolic process
metabolic process
ncRNA metabolic process
RNA metabolic process
translation
tRNA aminoacylation
tRNA aminoacylation for protein translation
tRNA metabolic process
Gene Properties
Blattner:b4129
Gene OrientationCounterclockwise
Centisome Percentage:93.78
Left Sequence End4351223
Right Sequence End4352740
Gene Sequence:
>1518 bp
ATGGCACAGATTGATTTCCGAAAAAAAATAAACTGGCATCGTCGTTACCGTTCACCGCAG
GGCGTTAAAACCGAACATGAGATCCTGCGGATCTTCGAGAGCGATCGCGGGCGTATCATC
AACTCTCCGGCAATTCGTCGTCTGCAACAAAAGACCCAGGTTTTTCCACTGGAGCGCAAT
GCCGCCGTGCGCACGCGTCTTACCCACTCGATGGAAGTCCAGCAGGTGGGGCGCTACATC
GCCAAAGAAATTTTAAGCCGTCTGAAAGAGCTTAAATTACTGGAAGCATACGGCCTGGAT
GAACTGACCGGTCCCTTTGAAAGCATTGTTGAGATGTCATGCCTGATGCACGATATCGGC
AATCCGCCGTTTGGTCATTTTGGCGAAGCGGCGATAAATGACTGGTTTCGCCAACGTTTG
CACCCGGAAGATGCCGAAAGCCAGCCTCTGACTGACGATCGCTGCAGCGTGGCGGCACTA
CGTTTACGGGACGGGGAAGAACCGCTTAACGAGCTGCGGCGCAAGATTCGTCAGGACTTA
TGTCATTTTGAGGGGAATGCACAAGGCATTCGCCTGGTGCATACATTGATGCGGATGAAT
CTCACCTGGGCACAGGTTGGCGGTATTTTAAAATATACCCGTCCGGCGTGGTGGCGTGGC
GAAACGCCTGAGACACATCACTATTTAATGAAAAAGCCGGGTTATTATCTTTCTGAAGAA
GCCTATATTGCCCGGTTGCGTAAAGAACTTAATTTGGCGCTTTACAGTCGTTTTCCATTA
ACGTGGATTATGGAAGCTGCCGACGACATCTCCTATTGTGTGGCAGACCTTGAAGATGCG
GTAGAGAAAAGAATATTTACCGTTGAGCAGCTTTATCATCATTTGCACGAAGCGTGGGGC
CAGCATGAGAAAGGTTCGCTCTTTTCGCTGGTGGTTGAAAATGCCTGGGAAAAATCACGC
TCAAATAGTTTAAGCCGCAGTACGGAAGATCAGTTTTTTATGTATTTACGGGTAAACACC
CTAAATAAACTGGTACCCTACGCGGCACAACGATTTATTGATAATCTGCCTGCGATTTTC
GCCGGAACGTTTAATCATGCATTATTGGAAGATGCCAGCGAATGCAGCGATCTTCTTAAG
CTATATAAAAATGTCGCTGTAAAACATGTGTTTAGCCATCCAGATGTCGAGCGGCTTGAA
TTGCAGGGCTATCGGGTCATTAGCGGATTATTAGAGATTTATCGTCCTTTATTAAGCCTG
TCGTTATCAGACTTTACTGAACTGGTAGAAAAAGAACGGGTGAAACGTTTCCCTATTGAA
TCGCGCTTATTCCACAAACTCTCGACGCGCCATCGGCTGGCCTATGTCGAGGCTGTCAGT
AAATTACCGTCAGATTCTCCTGAGTTTCCGCTATGGGAATATTATTACCGTTGCCGCCTG
CTGCAGGATTATATCAGCGGTATGACCGACCTCTATGCGTGGGATGAATACCGACGTCTG
ATGGCCGTAGAACAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:505
Protein Molecular Weight:57826
Protein Theoretical pI:5
PDB File:1E24
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Lysyl-tRNA synthetase, heat inducible
MSEQETRGANEAIDFNDELRNRREKLAALRQQGVAFPNDFRRDHTSDQLHEEFDAKDNQE
LESLNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYNDQFKKWDLGD
IIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDKFHGLQDQEVRYRQRYLDLIANDKS
RQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGASARPFITHHNALDLDMYLRIAP
ELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRT
LAQEVLGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIGI
TVEKSWGLGRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGG
REIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYGLPPTAGLGIGID
RMIMLFTNSHTIRDVILFPAMRPQK
References
External Links:
ResourceLink
Uniprot ID:P0A8N5
Uniprot Name:SYK2_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21239016
PDB ID:1E24
Ecogene ID:EG10553
Ecocyc:EG10553
ColiBase:b4129
Kegg Gene:b4129
EchoBASE ID:EB0548
CCDB:SYK2_ECOLI
BacMap:16131955
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Clark, R. L., Neidhardt, F. C. (1990). "Roles of the two lysyl-tRNA synthetases of Escherichia coli: analysis of nucleotide sequences and mutant behavior." J Bacteriol 172:3237-3243. Pubmed: 2188953
  • Desogus, G., Todone, F., Brick, P., Onesti, S. (2000). "Active site of lysyl-tRNA synthetase: structural studies of the adenylation reaction." Biochemistry 39:8418-8425. Pubmed: 10913247
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Leveque, F., Plateau, P., Dessen, P., Blanquet, S. (1990). "Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species." Nucleic Acids Res 18:305-312. Pubmed: 2183178
  • Onesti, S., Miller, A. D., Brick, P. (1995). "The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli." Structure 3:163-176. Pubmed: 7735833
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842