Difference between revisions of "TapA"
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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]]}}, | ||
+ | {{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=yqxM_2554486_2555247_-1 tapA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yqxM_2554486_2555247_-1 tapA] {{PubMed|22383849}} | ||
− | * '''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] |
* '''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}} | ||
+ | ** [[RemA]]: transcription activation {{PubMed|23646920}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
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<pubmed> 21488983 </pubmed> | <pubmed> 21488983 </pubmed> | ||
==Original publications== | ==Original publications== | ||
− | + | <pubmed>18430133,18047568,18647168, 20351052,16430695,10464223,17720793, 19605685 20431016 10559173 21477127 21856853 21815947 23646920</pubmed> | |
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− | <pubmed>18430133,18047568,18647168, 20351052,16430695,10464223,17720793, 19605685 20431016 10559173 21477127 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 15:19, 24 May 2013
- Description: required for the anchoring of the TasA amyloid fibers to the cell and for the initiation of fiber polymerization, minor fiber component
Gene name | tapA |
Synonyms | yqhD, yqxM |
Essential | no |
Product | TasA anchoring/assembly protein |
Function | biofilm formation |
Gene expression levels in SubtiExpress: tapA | |
Interactions involving this protein in SubtInteract: TapA | |
Regulation of this protein in SubtiPathways: Biofilm, Protein secretion | |
MW, pI | 28 kDa, 6.677 |
Gene length, protein length | 759 bp, 253 aa |
Immediate neighbours | sipW, yqzG |
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
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: BSU24640
Phenotypes of a mutant
The mutants are able to form a biofilm in the presence of D-amino acids PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: D-amino acids lead to disappearance of TapA from the cell wall PubMed
Database entries
- Structure:
- UniProt: P40949
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
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)
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)
Ilana Kolodkin-Gal, Diego Romero, Shugeng Cao, Jon Clardy, Roberto Kolter, Richard Losick
D-amino acids trigger biofilm disassembly.
Science: 2010, 328(5978);627-9
[PubMed:20431016]
[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)
Daniel López, Hera Vlamakis, Richard Losick, Roberto Kolter
Paracrine signaling in a bacterium.
Genes Dev: 2009, 23(14);1631-8
[PubMed:19605685]
[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)
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)