Pel

• Description: pectate lyase C
  
  

Gene name	pel
Synonyms
Essential	no
Product	pectate lyase C
Function	degradation of polygalacturonic acid
Gene expression levels in SubtiExpress: pel
MW, pI	45 kDa, 8.421
Gene length, protein length	1260 bp, 420 aa
Immediate neighbours	yflT, yflS
Sequences	Protein DNA Advanced_DNA
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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)