LysS

• Description: lysyl-tRNA synthetase
  
  

Gene name	lysS
Synonyms
Essential	yes PubMed
Product	lysyl-tRNA synthetase
Function	translation
Gene expression levels in SubtiExpress: lysS
Metabolic function and regulation of this protein in SubtiPathways: lysS
MW, pI	57 kDa, 5.034
Gene length, protein length	1497 bp, 499 aa
Immediate neighbours	yacF, rrnJ-16S
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation, essential genes

The gene

Basic information

• Locus tag: BSU00820

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU00820

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU00820

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

• UniProt: P37477

• KEGG entry: [3]

• E.C. number: 6.1.1.6

Expression and regulation

• Operon: pabB-pabA-pabC-sul-folB-folK-yazB-yacF-lysS PubMed

lysS PubMed

• Expression browser: lysS PubMed

• Sigma factor: pabB: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1972 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 7155 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)