Difference between revisions of "DltC"
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P39579 P39579] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P39579 P39579] | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU38520] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/6.1.1.13 6.1.1.13] | * '''E.C. number:''' [http://www.expasy.org/enzyme/6.1.1.13 6.1.1.13] |
Revision as of 01:58, 25 June 2009
- Description: D-alanine carrier protein
Gene name | dltC |
Synonyms | ipa-3r |
Essential | no |
Product | D-alanine carrier protein |
Function | biosynthesis of teichoic acid |
MW, pI | 8 kDa, 3.621 |
Gene length, protein length | 234 bp, 78 aa |
Immediate neighbours | dltB, dltD |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU38520
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate) (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry: P39579
- KEGG entry: [3]
- E.C. number: 6.1.1.13
Additional information
Expression and 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
Juergen J May, Robert Finking, Frank Wiegeshoff, Thomas T Weber, Nina Bandur, Ulrich Koert, Mohamed A Marahiel
Inhibition of the D-alanine:D-alanyl carrier protein ligase from Bacillus subtilis increases the bacterium's susceptibility to antibiotics that target the cell wall.
FEBS J: 2005, 272(12);2993-3003
[PubMed:15955059]
[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)
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)