Difference between revisions of "TapA"
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* '''Locus tag:''' BSU24640 | * '''Locus tag:''' BSU24640 | ||
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===Phenotypes of a mutant === | ===Phenotypes of a mutant === |
Revision as of 12:25, 26 January 2012
- Description: required for the anchoring of the TasA amyloid fibers to the cell and for the initiation of fiber polymerization, minor fiber component
Gene name | tapA |
Synonyms | yqhD, yqxM |
Essential | no |
Product | TasA anchoring/assembly protein |
Function | biofilm formation |
Interactions involving this protein in SubtInteract: TapA | |
Regulation of this protein in SubtiPathways: Biofilm, Protein secretion | |
MW, pI | 28 kDa, 6.677 |
Gene length, protein length | 759 bp, 253 aa |
Immediate neighbours | sipW, yqzG |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
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Contents
Categories containing this gene/protein
biofilm formation, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU24640
Phenotypes of a mutant
The mutants are able to form a biofilm in the presence of D-amino acids PubMed
Database entries
- 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:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: D-amino acids lead to disappearance of TapA from the cell wall PubMed
- Localization:
- attached to the cell surface (on the outside of the cell), associated with peptidoglycan PubMed
- secretion requires SipW
Database entries
- Structure:
- UniProt: P40949
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Original publications
Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J A Novel Factor Controlling Bistability in Bacillus subtilis: The YmdB Protein Affects Flagellin Expression and Biofilm Formation. J Bacteriol.: 2011, 193(21):5997-6007. PubMed:21856853
Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol Microbiol. 2011 81(6): 1459-1473. PubMed:21815947