Difference between revisions of "SipW"
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU24630 sipW] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU24630 sipW] | ||
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− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=SipW SipW] |
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/biofilm.html Biofilm], [http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/biofilm.html Biofilm], [http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]''' |
Revision as of 08:50, 12 November 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
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:
- Localization:
- membrane PubMed
Database entries
- Structure:
- UniProt: P54506
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- 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
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)