Difference between revisions of "LicC"

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<pubmed>19087206,8990303,16872404,,10438772,10627040 8990303, </pubmed>
 
<pubmed>19087206,8990303,16872404,,10438772,10627040 8990303, </pubmed>
# Reizer et al. (1999) Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of ''Bacillus subtilis''. ''Microbiology'' '''145:''' 3419-3429 [http://www.ncbi.nlm.nih.gov/pubmed/10627040 PubMed]
 
 
# Tobisch, S., P. Glaser, S. Krüger, and M. Hecker. 1997. Identification and characterization of a new ß-glucoside utilization system in ''Bacillus subtilis''. J. Bacteriol. 179:496-506. [http://www.ncbi.nlm.nih.gov/sites/entrez/8990303 PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 

Revision as of 13:39, 15 June 2009

  • Description: lichenan-specific phosphotransferase system, EIIC component

Gene name licC
Synonyms celB
Essential no
Product lichenan-specific phosphotransferase system,
EIIC component
Function lichenan uptake and phosphorylation
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 48 kDa, 8.584
Gene length, protein length 1356 bp, 452 aa
Immediate neighbours licA, licB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
LicC context.gif
This image was kindly provided by SubtiList




The gene

Basic information

  • Locus tag: BSU38580

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: PTS permease, lactose permease (Lac) family PubMed
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation: repressed by glucose (CcpA) , carbon catabolite repression, induction by oligomeric ß-glucosides PubMed
  • Regulatory mechanism: CcpA: transcription repression, catabolite repression: repression by CcpA, induction: transcription activation by the PRD-type regulator LicR PubMed
  • 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

Takashi Inaoka, Takenori Satomura, Yasutaro Fujita, Kozo Ochi
Novel gene regulation mediated by overproduction of secondary metabolite neotrehalosadiamine in Bacillus subtilis.
FEMS Microbiol Lett: 2009, 291(2);151-6
[PubMed:19087206] [WorldCat.org] [DOI] (I p)

Le Thi Tam, Christine Eymann, Dirk Albrecht, Rabea Sietmann, Frieder Schauer, Michael Hecker, Haike Antelmann
Differential gene expression in response to phenol and catechol reveals different metabolic activities for the degradation of aromatic compounds in Bacillus subtilis.
Environ Microbiol: 2006, 8(8);1408-27
[PubMed:16872404] [WorldCat.org] [DOI] (P p)

Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[PubMed:10627040] [WorldCat.org] [DOI] (P p)

S Tobisch, J Stülke, M Hecker
Regulation of the lic operon of Bacillus subtilis and characterization of potential phosphorylation sites of the LicR regulator protein by site-directed mutagenesis.
J Bacteriol: 1999, 181(16);4995-5003
[PubMed:10438772] [WorldCat.org] [DOI] (P p)

S Tobisch, P Glaser, S Krüger, M Hecker
Identification and characterization of a new beta-glucoside utilization system in Bacillus subtilis.
J Bacteriol: 1997, 179(2);496-506
[PubMed:8990303] [WorldCat.org] [DOI] (P p)