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
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

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

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
  • RemA: transcription activation 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:
  • 1A937 ( sipW::kan), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Beth Lazazzera, Los Angeles, USA

References

Reviews

Ross E Dalbey, Peng Wang, Jan Maarten van Dijl
Membrane proteases in the bacterial protein secretion and quality control pathway.
Microbiol Mol Biol Rev: 2012, 76(2);311-30
[PubMed:22688815] [WorldCat.org] [DOI] (I p)

Jan Maarten van Dijl
Biofilm research uncovers a novel nonenzymatic signal peptidase function in Bacillus.
J Bacteriol: 2012, 194(11);2779-80
[PubMed:22427624] [WorldCat.org] [DOI] (I p)

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

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)