Difference between revisions of "LicB"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU38590&redirect=T BSU38590]
  
 
* '''DBTBS entry:''' no entry
 
* '''DBTBS entry:''' no entry
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU38590&redirect=T BSU38590]
  
 
* '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=1e2b 1e2b] (from ''E. coli'', 40% identity) {{PubMed|9041631}}
 
* '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=1e2b 1e2b] (from ''E. coli'', 40% identity) {{PubMed|9041631}}

Revision as of 15:09, 2 April 2014

Gene name licB
Synonyms celA
Essential no
Product trigger enzyme: lichenan-specific
phosphotransferase system, EIIB component
Function lichenan uptake and phosphorylation,
control of LicR activity
Gene expression levels in SubtiExpress: licB
Interactions involving this protein in SubtInteract: LicB
Metabolic function and regulation of this protein in SubtiPathways:
licB
MW, pI 10 kDa, 6.314
Gene length, protein length 306 bp, 102 aa
Immediate neighbours licC, licR
Sequences Protein DNA DNA_with_flanks
Genetic context
LicB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LicB expression.png















Categories containing this gene/protein

phosphotransferase systems, utilization of specific carbon sources, transcription factors and their control, trigger enzyme, phosphoproteins

This gene is a member of the following regulons

CcpA regulon, LicR regulon

The gene

Basic information

  • Locus tag: BSU38590

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 EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate (according to Swiss-Prot)
  • Protein family: PTS permease, lactose permease (Lac) family PubMed
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification: phosphorylation on Ser-37 PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 1e2b (from E. coli, 40% identity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Regulation:
  • 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)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P 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)

E Ab, G Schuurman-Wolters, J Reizer, M H Saier, K Dijkstra, R M Scheek, G T Robillard
The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.
Protein Sci: 1997, 6(2);304-14
[PubMed:9041631] [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)