Difference between revisions of "DltE"
Line 37: | Line 37: | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
− | + | <br/><br/> | |
= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
Line 59: | Line 59: | ||
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
+ | * more sensitive to nisin {{PubMed|23980836}} | ||
=== Database entries === | === Database entries === | ||
Line 115: | Line 116: | ||
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=dltE_3956492_3957250_1 dltE] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=dltE_3956492_3957250_1 dltE] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' [[SigD]] {{PubMed|7797557}}, [[SigM]] {{PubMed|18179421}}, [[SigX]] {{PubMed|14762009}} | + | * '''[[Sigma factor]]:''' [[SigD]] {{PubMed|7797557}}, [[SigM]] {{PubMed|18179421}}, [[SigX]] {{PubMed|14762009}} |
* '''Regulation:''' | * '''Regulation:''' | ||
Line 147: | Line 148: | ||
=References= | =References= | ||
− | + | <pubmed>14762009,,7797557, 23980836 21856855,21926231</pubmed> | |
− | <pubmed>14762009,,7797557, </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 18:15, 30 August 2013
- Description: D-alanine transfer from undecaprenol-phosphate to the poly(glycerophosphate) chain, alanylation of teichoic acid provides some resistance against positively charged antimicrobial peptides
Gene name | dltE |
Synonyms | ipa-1r |
Essential | no |
Product | D-alanine transfer from undecaprenol-phosphate to the poly(glycerophosphate) chain |
Function | biosynthesis of teichoic acid |
Gene expression levels in SubtiExpress: dltE | |
MW, pI | 28 kDa, 5.095 |
Gene length, protein length | 756 bp, 252 aa |
Immediate neighbours | dltD, ywaA |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
cell wall synthesis, biosynthesis of cell wall components, cell envelope stress proteins (controlled by SigM, V, W, X, Y)
This gene is a member of the following regulons
SigD regulon, SigM regulon, SigX regulon, Spo0A regulon, stringent response, YvrHb regulon
The gene
Basic information
- Locus tag: BSU38540
Phenotypes of a mutant
- more sensitive to nisin PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: short-chain dehydrogenases/reductases (SDR) family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P39577
- KEGG entry: [3]
- E.C. number:
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
Anthony W Kingston, Xiaojie Liao, John D Helmann
Contributions of the σ(W) , σ(M) and σ(X) regulons to the lantibiotic resistome of Bacillus subtilis.
Mol Microbiol: 2013, 90(3);502-18
[PubMed:23980836]
[WorldCat.org]
[DOI]
(I p)
Veronica Guariglia-Oropeza, John D Helmann
Bacillus subtilis σ(V) confers lysozyme resistance by activation of two cell wall modification pathways, peptidoglycan O-acetylation and D-alanylation of teichoic acids.
J Bacteriol: 2011, 193(22);6223-32
[PubMed:21926231]
[WorldCat.org]
[DOI]
(I p)
Theresa D Ho, Jessica L Hastie, Peter J Intile, Craig D Ellermeier
The Bacillus subtilis extracytoplasmic function σ factor σ(V) is induced by lysozyme and provides resistance to lysozyme.
J Bacteriol: 2011, 193(22);6215-22
[PubMed:21856855]
[WorldCat.org]
[DOI]
(I p)
Min Cao, John D Helmann
The Bacillus subtilis extracytoplasmic-function sigmaX factor regulates modification of the cell envelope and resistance to cationic antimicrobial peptides.
J Bacteriol: 2004, 186(4);1136-46
[PubMed:14762009]
[WorldCat.org]
[DOI]
(P p)
M Perego, P Glaser, A Minutello, M A Strauch, K Leopold, W Fischer
Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation.
J Biol Chem: 1995, 270(26);15598-606
[PubMed:7797557]
[WorldCat.org]
[DOI]
(P p)