Difference between revisions of "SipW"

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* '''Description:''' signal peptidase I, required for biofilm formation <br/><br/>
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* '''Description:''' signal peptidase I, processes [[TasA]] and [[TapA]], required for [[biofilm formation]] <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 570 bp, 190 aa  
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 570 bp, 190 aa  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[tasA]]'', ''[[yqxM]]''
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[tasA]]'', ''[[tapA]]''
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14394&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14394&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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=== Additional information===
 
=== Additional information===
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−
 
  
  
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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
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* '''Catalyzed reaction/ biological activity:''' Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins (according to Swiss-Prot)
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* '''Catalyzed reaction/ biological activity:''' Cleavage of hydrophobic, N-terminal signal or leader sequences from [[TasA]] and [[TapA]]
  
 
* '''Protein family:''' peptidase S26B family (according to Swiss-Prot)
 
* '''Protein family:''' peptidase S26B family (according to Swiss-Prot)
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* '''Interactions:'''
 
* '''Interactions:'''
  
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* '''Localization:''' secreted (according to Swiss-Prot)
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* '''Localization:''' membrane
  
 
=== Database entries ===
 
=== Database entries ===
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=Expression and regulation=
 
=Expression and regulation=
  
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* '''Operon:''' ''[[yqxM]]-[[sipW]]-[[tasA]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/16430695 PubMed]
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* '''Operon:''' ''[[tapA]]-[[sipW]]-[[tasA]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/16430695 PubMed]
  
 
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/16430695 PubMed]
 
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/16430695 PubMed]
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=References=
 
=References=
  
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<pubmed>18047568,15175311,16430695,10368135,9694797,18430133,18647168,10464223,17720793, 20351052 10827084 </pubmed>
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<pubmed>18047568,15175311,16430695,10368135,9694797,18430133,18647168,10464223,17720793, 20351052 10827084 21477127 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 07:44, 12 April 2011

Gene name sipW
Synonyms yqhE
Essential no
Product signal peptidase I
Function biofilm formation
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
SipW context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

protein secretion, biofilm formation

This gene is a member of the following regulons

AbrB regulon, SinR regulon

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: Cleavage of hydrophobic, N-terminal signal or leader sequences from TasA and TapA
  • 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:
  • Localization: membrane

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Diego Romero, Hera Vlamakis, Richard Losick, Roberto Kolter
An accessory protein required for anchoring and assembly of amyloid fibres in B. subtilis biofilms.
Mol Microbiol: 2011, 80(5);1155-68
[PubMed:21477127] [WorldCat.org] [DOI] (I p)

Yunrong Chai, Thomas Norman, Roberto Kolter, Richard Losick
An epigenetic switch governing daughter cell separation in Bacillus subtilis.
Genes Dev: 2010, 24(8);754-65
[PubMed:20351052] [WorldCat.org] [DOI] (I p)

Kazuo Kobayashi
SlrR/SlrA controls the initiation of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 69(6);1399-410
[PubMed:18647168] [WorldCat.org] [DOI] (I p)

Frances Chu, Daniel B Kearns, Anna McLoon, Yunrong Chai, Roberto Kolter, Richard Losick
A novel regulatory protein governing biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 68(5);1117-27
[PubMed:18430133] [WorldCat.org] [DOI] (I p)

Yunrong Chai, Frances Chu, Roberto Kolter, Richard Losick
Bistability and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 67(2);254-63
[PubMed:18047568] [WorldCat.org] [DOI] (P p)

Mark A Strauch, Benjamin G Bobay, John Cavanagh, Fude Yao, Angelo Wilson, Yoann Le Breton
Abh and AbrB control of Bacillus subtilis antimicrobial gene expression.
J Bacteriol: 2007, 189(21);7720-32
[PubMed:17720793] [WorldCat.org] [DOI] (P p)

Frances Chu, Daniel B Kearns, Steven S Branda, Roberto Kolter, Richard Losick
Targets of the master regulator of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2006, 59(4);1216-28
[PubMed:16430695] [WorldCat.org] [DOI] (P p)

Steven S Branda, José Eduardo González-Pastor, Etienne Dervyn, S Dusko Ehrlich, Richard Losick, Roberto Kolter
Genes involved in formation of structured multicellular communities by Bacillus subtilis.
J Bacteriol: 2004, 186(12);3970-9
[PubMed:15175311] [WorldCat.org] [DOI] (P p)

H Tjalsma, A G Stover, A Driks, G Venema, S Bron, J M van Dijl
Conserved serine and histidine residues are critical for activity of the ER-type signal peptidase SipW of Bacillus subtilis.
J Biol Chem: 2000, 275(33);25102-8
[PubMed:10827084] [WorldCat.org] [DOI] (P p)

A G Stöver, A Driks
Regulation of synthesis of the Bacillus subtilis transition-phase, spore-associated antibacterial protein TasA.
J Bacteriol: 1999, 181(17);5476-81
[PubMed:10464223] [WorldCat.org] [DOI] (P p)

M Serrano, R Zilhão, E Ricca, A J Ozin, C P Moran, A O Henriques
A Bacillus subtilis secreted protein with a role in endospore coat assembly and function.
J Bacteriol: 1999, 181(12);3632-43
[PubMed:10368135] [WorldCat.org] [DOI] (P p)

H Tjalsma, A Bolhuis, M L van Roosmalen, T Wiegert, W Schumann, C P Broekhuizen, W J Quax, G Venema, S Bron, J M van Dijl
Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases.
Genes Dev: 1998, 12(15);2318-31
[PubMed:9694797] [WorldCat.org] [DOI] (P p)

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