Difference between revisions of "DltD"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU38530&redirect=T BSU38530] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/dltABCDE.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/dltABCDE.html] | ||
Line 94: | Line 95: | ||
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU38530&redirect=T BSU38530] | ||
* '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=3bma 3BMA] (from ''Streptococcus pneumoniae'', 26% identity) | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=3bma 3BMA] (from ''Streptococcus pneumoniae'', 26% identity) |
Revision as of 15:08, 2 April 2014
- 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 | dltD |
Synonyms | ipa-2r |
Essential | no |
Product | D-alanine transfer from undecaprenol-phosphate to the poly(glycerophosphate) chain |
Function | biosynthesis of teichoic acid |
Gene expression levels in SubtiExpress: dltD | |
MW, pI | 44 kDa, 9.858 |
Gene length, protein length | 1176 bp, 392 aa |
Immediate neighbours | dltC, dltE |
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: BSU38530
Phenotypes of a mutant
- more sensitive to nisin PubMed
Database entries
- BsubCyc: BSU38530
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU38530
- Structure: 3BMA (from Streptococcus pneumoniae, 26% identity)
- UniProt: P39578
- 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)
Hanne-Leena Hyyryläinen, Milla Pietiäinen, Tuula Lundén, Anna Ekman, Marika Gardemeister, Sanna Murtomäki-Repo, Haike Antelmann, Michael Hecker, Leena Valmu, Matti Sarvas, Vesa P Kontinen
The density of negative charge in the cell wall influences two-component signal transduction in Bacillus subtilis.
Microbiology (Reading): 2007, 153(Pt 7);2126-2136
[PubMed:17600057]
[WorldCat.org]
[DOI]
(P 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)
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)
H L Hyyrylainen, M Vitikainen, J Thwaite, H Wu, M Sarvas, C R Harwood, V P Kontinen, K Stephenson
D-Alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis.
J Biol Chem: 2000, 275(35);26696-703
[PubMed:10871614]
[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)