Difference between revisions of "TapA"

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(Extended information on the protein)
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* '''Effectors of protein activity:''' D-amino acids lead to disappearance of TapA from the cell wall {{PubMed|21477127}}
 
* '''Effectors of protein activity:''' D-amino acids lead to disappearance of TapA from the cell wall {{PubMed|21477127}}
  
* '''Interactions:''' [[TapA]]-[[TasA]] {{PubMed|21477127}}
+
* '''[[SubtInteract|Interactions]]:'''
 +
** [[TapA]]-[[TasA]] {{PubMed|21477127}}
  
* '''Localization:'''  
+
* '''[[Localization]]:'''  
 
** attached to the cell surface (on the outside of the cell), associated with peptidoglycan  {{PubMed|21477127}}
 
** attached to the cell surface (on the outside of the cell), associated with peptidoglycan  {{PubMed|21477127}}
 
** secretion requires SipW
 
** secretion requires SipW

Revision as of 11:47, 10 August 2011

  • 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
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
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YqxM context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biofilm formation, membrane proteins

This gene is a member of the following regulons

AbrB 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
  • Localization:
    • attached to the cell surface (on the outside of the cell), associated with peptidoglycan PubMed
    • secretion requires SipW

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

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

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)