Pel

• Description: pectate lyase C
  
  

Gene name	pel
Synonyms
Essential	no
Product	pectate lyase C
Function	degradation of polygalacturonic acid
MW, pI	45 kDa, 8.421
Gene length, protein length	1260 bp, 420 aa
Immediate neighbours	yflT, yflS
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

CcpA regulon, ComA regulon, TnrA regulon

The gene

Basic information

• Locus tag: BSU07560

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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 1 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:
  • extracellular (signal peptide), major constituent of the secretome PubMed

Database entries

• Structure: 2O1D (bound to trisaccharide), 1BN8

• UniProt: P39116

• KEGG entry: [3]

• E.C. number: 4.2.2.2

Expression and regulation

• Operon: pel PubMed

• Expression browser: pel PubMed

• Sigma factor:

• Regulation:
  • repressed by glucose (3.8-fold) (CcpA) PubMed
  • repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
  • expressed at high cell density (ComA) PubMed

• Regulatory mechanism:
  • ComA: transcription activation (ComA) PubMed
  • CcpA: transcription repression
  • TnrA: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

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)

Natalia Comella, Alan D Grossman
Conservation of genes and processes controlled by the quorum response in bacteria: characterization of genes controlled by the quorum-sensing transcription factor ComA in Bacillus subtilis.
Mol Microbiol: 2005, 57(4);1159-74
[PubMed:16091051] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818] [WorldCat.org] [DOI] (P p)

W Nasser, A C Awadé, S Reverchon, J Robert-Baudouy
Pectate lyase from Bacillus subtilis: molecular characterization of the gene, and properties of the cloned enzyme.
FEBS Lett: 1993, 335(3);319-26
[PubMed:8262178] [WorldCat.org] [DOI] (P p)