Difference between revisions of "SipW"
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Revision as of 13:54, 16 May 2013
- Description: bifunctional signal peptidase I that controls surface-adhered biofilm formation and processes TasA and TapA
Gene name | sipW |
Synonyms | yqhE |
Essential | no |
Product | signal peptidase I |
Function | biofilm formation |
Gene expression levels in SubtiExpress: sipW | |
Interactions involving this protein in SubtInteract: SipW | |
Regulation of this protein in SubtiPathways: Biofilm, Protein secretion | |
MW, pI | 20 kDa, 5.494 |
Gene length, protein length | 570 bp, 190 aa |
Immediate neighbours | tasA, tapA |
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
protein secretion, biofilm formation, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU24630
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- important for biofilm formation on a solid surface, but not required at an air-liquid interface PubMed
- Cleavage of hydrophobic, N-terminal signal or leader sequences from TasA and TapA PubMed
- Protein family: peptidase S26B family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- membrane PubMed
Database entries
- Structure:
- UniProt: P54506
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Beth Lazazzera, Los Angeles, USA
Your additional remarks
References
Reviews
Additional reviews: PubMed
Adam Driks
Tapping into the biofilm: insights into assembly and disassembly of a novel amyloid fibre in Bacillus subtilis.
Mol Microbiol: 2011, 80(5);1133-6
[PubMed:21488983]
[WorldCat.org]
[DOI]
(I p)
Original publications
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
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