SipW

• 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
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

protein secretion, biofilm formation, membrane proteins

This gene is a member of the following regulons

AbrB regulon, SinR regulon

The gene

Basic information

• Locus tag: BSU24630

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:
  • SipW-TapA PubMed
  • SipW-TasA PubMed

• Localization:
  • membrane PubMed

Database entries

• Structure:

• UniProt: P54506

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: tapA-sipW-tasA PubMed

• Expression browser: sipW PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by SinR PubMed
  • repressed during logrithmic growth (AbrB) PubMed

• Regulatory mechanism:
  • AbrB: transcription repression PubMed
  • SinR: transcription repression PubMed

• Additional information:
  • induction by sequestration of SinR by SinI or SlrA PubMed or by SlrR PubMed
  • the tapA-sipW-tasA operon is not expressed in a ymdB mutant PubMed
  • the amount of the mRNA is substantially decreased upon depletion of RNase Y (this is likely due to the increased stability of the sinR mRNA) PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Beth Lazazzera, Los Angeles, USA

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