Difference between revisions of "Pel"
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
− | * '''Localization:''' extracellular (signal peptide), major constituent of the secretome [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed] | + | * '''[[Localization]]:''' |
+ | ** extracellular (signal peptide), major constituent of the secretome [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed] | ||
=== Database entries === | === Database entries === |
Revision as of 17:38, 2 December 2011
- 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
|
Contents
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
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
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 1 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- extracellular (signal peptide), major constituent of the secretome PubMed
Database entries
- UniProt: P39116
- KEGG entry: [3]
- E.C. number: 4.2.2.2
Additional information
Expression and regulation
- Operon: pel PubMed
- 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
Reviews
Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481]
[WorldCat.org]
[DOI]
(I p)
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)