Difference between revisions of "SipW"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
 
{{SubtiWiki regulon|[[AbrB regulon]]}},
 
{{SubtiWiki regulon|[[AbrB regulon]]}},
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{{SubtiWiki regulon|[[RemA regulon]]}},
 
{{SubtiWiki regulon|[[SinR regulon]]}}
 
{{SubtiWiki regulon|[[SinR regulon]]}}
  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sipW_2553930_2554502_-1 sipW] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sipW_2553930_2554502_-1 sipW] {{PubMed|22383849}}
  
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* '''Sigma factor:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/16430695 PubMed]
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* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/16430695 PubMed]
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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** [[AbrB]]:  transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/10464223,17720793 PubMed]
 
** [[AbrB]]:  transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/10464223,17720793 PubMed]
 
** [[SinR]]: transcription repression {{PubMed|16430695}}
 
** [[SinR]]: transcription repression {{PubMed|16430695}}
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** [[RemA]]: transcription activation {{PubMed|23646920}}
  
 
* '''Additional information:'''  
 
* '''Additional information:'''  
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=References=
 
=References=
 
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'''Additional reviews:''' {{PubMed|22427624}}
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<pubmed>21488983 22427624</pubmed>
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<pubmed>21488983</pubmed>
 
  
 
==Original publications==
 
==Original publications==
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<pubmed> 22328672</pubmed>
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<pubmed> 22328672 18047568,15175311,16430695,10368135,9694797,18430133,18647168,10464223,17720793, 20351052 10827084 21477127 10559173 23646920 21856853 21815947</pubmed>
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<big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J''  </big>
 
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<big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big>
 
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<big>Mol Microbiol. 2011 81(6): 1459-1473. </big>
 
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[http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947]
 
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<big>''Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J''  </big>
 
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<big>'''A Novel Factor Controlling Bistability in ''Bacillus subtilis'': The YmdB Protein Affects</big>
 
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<big>Flagellin Expression and Biofilm Formation.''' </big>
 
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<big>J Bacteriol.: 2011, 193(21):5997-6007. </big>
 
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[http://www.ncbi.nlm.nih.gov/pubmed/21856853 PubMed:21856853]
 
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<pubmed>18047568,15175311,16430695,10368135,9694797,18430133,18647168,10464223,17720793, 20351052 10827084 21477127 10559173 </pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:18, 24 May 2013

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
SipW context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SipW expression.png















Categories containing this gene/protein

protein secretion, biofilm formation, membrane proteins

This gene is a member of the following regulons

AbrB regulon, RemA 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:
    • 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:

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

Reviews


Original publications

Jared T Winkelman, Anna C Bree, Ashley R Bate, Patrick Eichenberger, Richard L Gourse, Daniel B Kearns
RemA is a DNA-binding protein that activates biofilm matrix gene expression in Bacillus subtilis.
Mol Microbiol: 2013, 88(5);984-97
[PubMed:23646920] [WorldCat.org] [DOI] (I p)

Rebecca Terra, Nicola R Stanley-Wall, Guoqiang Cao, Beth A Lazazzera
Identification of Bacillus subtilis SipW as a bifunctional signal peptidase that controls surface-adhered biofilm formation.
J Bacteriol: 2012, 194(11);2781-90
[PubMed:22328672] [WorldCat.org] [DOI] (I p)

Christine Diethmaier, Nico Pietack, Katrin Gunka, Christoph Wrede, Martin Lehnik-Habrink, Christina Herzberg, Sebastian Hübner, Jörg Stülke
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] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

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
Control of synthesis and secretion of the Bacillus subtilis protein YqxM.
J Bacteriol: 1999, 181(22);7065-9
[PubMed:10559173] [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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