PelC

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  • Description: pectate lyase C

Gene name pelC
Synonyms yvpA
Essential no
Product pectate lyase C
Function degradation of polygalacturonic acid
MW, pI 24 kDa, 9.14
Gene length, protein length 663 bp, 221 aa
Immediate neighbours yvpB, yvoF
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YvpA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU34950

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends (according to Swiss-Prot)
  • Protein family: polysaccharide lyase 3 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: secreted (according to Swiss-Prot), extracellular (signal peptide) PubMed

Database entries

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • 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

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Margarita Soriano, Pilar Diaz, Francisco I Javier Pastor
Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin.
Microbiology (Reading): 2006, 152(Pt 3);617-625
[PubMed:16514142] [WorldCat.org] [DOI] (P p)