Difference between revisions of "TatAY"
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== Original publications == | == Original publications == | ||
− | <pubmed>15554971, 19383693 21479178 22041895 22767609 22383849 23180473 23256564 24652282 24875903 </pubmed> | + | <pubmed>15554971, 19383693 21479178 22041895 22767609 22383849 23180473 23256564 24652282 24875903 26239117</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 17:16, 5 August 2015
Gene name | tatAY |
Synonyms | ydiI |
Essential | no |
Product | component of the twin-arginine translocation pathway |
Function | TAT protein secretion |
Gene expression levels in SubtiExpress: tatAY | |
Interactions involving this protein in SubtInteract: TatAY | |
Metabolic function and regulation of this protein in SubtiPathways: TatAY | |
MW, pI | 5 kDa, 6.558 |
Gene length, protein length | 171 bp, 57 aa |
Immediate neighbours | rex, tatCY |
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, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU05980
Phenotypes of a mutant
Database entries
- BsubCyc: BSU05980
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: tatA/E family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- BsubCyc: BSU05980
- Structure:
- UniProt: O05522
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation: constitutitvely expressed PubMed
- Regulatory mechanism:
- Additional information:
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
Vivianne J Goosens, Alba De-San-Eustaquio-Campillo, Rut Carballido-López, Jan Maarten van Dijl
A Tat ménage à trois--The role of Bacillus subtilis TatAc in twin-arginine protein translocation.
Biochim Biophys Acta: 2015, 1853(10 Pt A);2745-53
[PubMed:26239117]
[WorldCat.org]
[DOI]
(P p)
Roshani Patel, Cvetelin Vasilev, Daniel Beck, Carmine G Monteferrante, Jan Maarten van Dijl, C Neil Hunter, Corinne Smith, Colin Robinson
A mutation leading to super-assembly of twin-arginine translocase (Tat) protein complexes.
Biochim Biophys Acta: 2014, 1843(9);1978-86
[PubMed:24875903]
[WorldCat.org]
[DOI]
(P p)
Vivianne J Goosens, Carmine G Monteferrante, Jan Maarten van Dijl
Co-factor insertion and disulfide bond requirements for twin-arginine translocase-dependent export of the Bacillus subtilis Rieske protein QcrA.
J Biol Chem: 2014, 289(19);13124-31
[PubMed:24652282]
[WorldCat.org]
[DOI]
(I p)
Vivianne J Goosens, Andreas Otto, Corinna Glasner, Carmine C Monteferrante, René van der Ploeg, Michael Hecker, Dörte Becher, Jan Maarten van Dijl
Novel twin-arginine translocation pathway-dependent phenotypes of Bacillus subtilis unveiled by quantitative proteomics.
J Proteome Res: 2013, 12(2);796-807
[PubMed:23256564]
[WorldCat.org]
[DOI]
(I p)
Carmine G Monteferrante, Calum MacKichan, Elodie Marchadier, Maria-Victoria Prejean, Rut Carballido-López, Jan Maarten van Dijl
Mapping the twin-arginine protein translocation network of Bacillus subtilis.
Proteomics: 2013, 13(5);800-11
[PubMed:23180473]
[WorldCat.org]
[DOI]
(I p)
Carmine G Monteferrante, Marcus Miethke, René van der Ploeg, Corinna Glasner, Jan Maarten van Dijl
Specific targeting of the metallophosphoesterase YkuE to the bacillus cell wall requires the twin-arginine translocation system.
J Biol Chem: 2012, 287(35);29789-800
[PubMed:22767609]
[WorldCat.org]
[DOI]
(I p)
Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849]
[WorldCat.org]
[DOI]
(I p)
René van der Ploeg, James P Barnett, Nishi Vasisht, Vivianne J Goosens, Dierk C Pöther, Colin Robinson, Jan Maarten van Dijl
Salt sensitivity of minimal twin arginine translocases.
J Biol Chem: 2011, 286(51);43759-43770
[PubMed:22041895]
[WorldCat.org]
[DOI]
(I p)
René van der Ploeg, Ulrike Mäder, Georg Homuth, Marc Schaffer, Emma L Denham, Carmine G Monteferrante, Marcus Miethke, Mohamed A Marahiel, Colin R Harwood, Theresa Winter, Michael Hecker, Haike Antelmann, Jan Maarten van Dijl
Environmental salinity determines the specificity and need for Tat-dependent secretion of the YwbN protein in Bacillus subtilis.
PLoS One: 2011, 6(3);e18140
[PubMed:21479178]
[WorldCat.org]
[DOI]
(I e)
Robyn T Eijlander, Magdalena A Kolbusz, Erwin M Berendsen, Oscar P Kuipers
Effects of altered TatC proteins on protein secretion efficiency via the twin-arginine translocation pathway of Bacillus subtilis.
Microbiology (Reading): 2009, 155(Pt 6);1776-1785
[PubMed:19383693]
[WorldCat.org]
[DOI]
(P p)
Jan D H Jongbloed, Ulrike Grieger, Haike Antelmann, Michael Hecker, Reindert Nijland, Sierd Bron, Jan Maarten van Dijl
Two minimal Tat translocases in Bacillus.
Mol Microbiol: 2004, 54(5);1319-25
[PubMed:15554971]
[WorldCat.org]
[DOI]
(P p)