LysS

From SubtiWiki
Revision as of 10:21, 7 August 2012 by Jstuelk (talk | contribs) (Reverted edits by 134.76.70.252 (talk) to last revision by Jstuelk)
Jump to: navigation, search
  • Description: lysyl-tRNA synthetase

Gene name lysS
Synonyms
Essential yes PubMed
Product lysyl-tRNA synthetase
Function translation
Metabolic function and regulation of this protein in SubtiPathways:
tRNA charging, Folate
MW, pI 57 kDa, 5.034
Gene length, protein length 1497 bp, 499 aa
Immediate neighbours yacF, rrnJ-16S
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
LysS context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

translation, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU00820

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys) (according to Swiss-Prot)
  • Protein family: class-II aminoacyl-tRNA synthetase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2E9I (from Geobacillus stearothermophilus, in complex with L-Lysine hydroxamate-AMP) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

lysS PubMed

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Haruko Sakurama, Teisuke Takita, Bunzo Mikami, Takafumi Itoh, Kiyoshi Yasukawa, Kuniyo Inouye
Two crystal structures of lysyl-tRNA synthetase from Bacillus stearothermophilus in complex with lysyladenylate-like compounds: insights into the irreversible formation of the enzyme-bound adenylate of L-lysine hydroxamate.
J Biochem: 2009, 145(5);555-63
[PubMed:19174549] [WorldCat.org] [DOI] (I p)

Antoine de Saizieu, Pierre Vankan, Cassandra Vockler, Adolphus P G M van Loon
The trp RNA-binding attenuation protein (TRAP) regulates the steady-state levels of transcripts of the Bacillus subtilis folate operon.
Microbiology (Reading): 1997, 143 ( Pt 3);979-989
[PubMed:9084182] [WorldCat.org] [DOI] (P p)