LuxS

• Description: S-ribosylhomocysteine lyase, autoinducer-2 production protein, required for swarming motility and biofilm formation
  
  

Gene name	luxS
Synonyms	ytjB
Essential	no
Product	S-ribosylhomocysteine lyase
Function	methionine salvage
Gene expression levels in SubtiExpress: luxS
Metabolic function and regulation of this protein in SubtiPathways: luxS
MW, pI	17 kDa, 5.168
Gene length, protein length	471 bp, 157 aa
Immediate neighbours	ytkA, ytjA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed 500px

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, motility and chemotaxis, quorum sensing, biofilm formation

The gene

Basic information

• Locus tag: BSU30670

Database entries

• BsubCyc: BSU30670

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione (according to Swiss-Prot)

• Protein family: luxS family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity: subject to feedback inhibition PubMed

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU30670

• Structure: 1JQW (complex with homocysteine), 1J98

• UniProt: O34667

• KEGG entry: [3]

• E.C. number: 4.4.1.21

Expression and regulation

• Operon: luxS PubMed

• Expression browser: luxS PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information: subject to feedback inhibition PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 2174 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 3894 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 2289 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1319 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2360 PubMed

Biological materials

• Mutant:
  • 1A953 ( luxS::cat), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532] [WorldCat.org] [DOI] (I p)

Esteban Lombardía, Adrián J Rovetto, Ana L Arabolaza, Roberto R Grau
A LuxS-dependent cell-to-cell language regulates social behavior and development in Bacillus subtilis.
J Bacteriol: 2006, 188(12);4442-52
[PubMed:16740951] [WorldCat.org] [DOI] (P p)

M T Hilgers, M L Ludwig
Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site.
Proc Natl Acad Sci U S A: 2001, 98(20);11169-74
[PubMed:11553770] [WorldCat.org] [DOI] (P p)

Alia Lapidus, Nathalie Galleron, Alexei Sorokin, S Dusko Ehrlich
Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region.
Microbiology (Reading): 1997, 143 ( Pt 11);3431-3441
[PubMed:9387221] [WorldCat.org] [DOI] (P p)