LicC

• 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 This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU38580

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions: LicB-LicC

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• Structure:

• Swiss prot entry: P46317

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: licB-licC-licA-licH PubMed

• Sigma factor: SigA PubMed

• 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:

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)

1. 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 PubMed

1. 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. PubMed
2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed