Difference between revisions of "TatCD"
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== Original publications == | == Original publications == | ||
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 16:46, 3 July 2015
Gene name | tatCD |
Synonyms | ycbT |
Essential | no |
Product | component of the twin-arginine translocation pathway |
Function | TAT protein secretion |
Gene expression levels in SubtiExpress: tatCD | |
Interactions involving this protein in SubtInteract: TatCD | |
Metabolic function and regulation of this protein in SubtiPathways: TatCD | |
MW, pI | 27 kDa, 9.342 |
Gene length, protein length | 735 bp, 245 aa |
Immediate neighbours | tatAD, pcp |
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
phosphate metabolism, protein secretion, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU02640
Phenotypes of a mutant
Database entries
- BsubCyc: BSU02640
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Protein family: tatC family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization: cell membrane PubMed
Database entries
- BsubCyc: BSU02640
- Structure:
- UniProt: P42252
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Oscar Kuipers, University of Groningen, The Netherlands Homepage
Your additional remarks
References
Reviews
Kenneth Cline
Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).
J Biol Chem: 2015, 290(27);16530-8
[PubMed:25975269]
[WorldCat.org]
[DOI]
(I p)
Vivianne J Goosens, Carmine G Monteferrante, Jan Maarten van Dijl
The Tat system of Gram-positive bacteria.
Biochim Biophys Acta: 2014, 1843(8);1698-706
[PubMed:24140208]
[WorldCat.org]
[DOI]
(P p)
Tracy Palmer, Ben C Berks
The twin-arginine translocation (Tat) protein export pathway.
Nat Rev Microbiol: 2012, 10(7);483-96
[PubMed:22683878]
[WorldCat.org]
[DOI]
(I e)
Original publications
Domenico Simone, Denice C Bay, Thorin Leach, Raymond J Turner
Diversity and evolution of bacterial twin arginine translocase protein, TatC, reveals a protein secretion system that is evolving to fit its environmental niche.
PLoS One: 2013, 8(11);e78742
[PubMed:24236045]
[WorldCat.org]
[DOI]
(I e)
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, Jacopo Baglieri, Colin Robinson, Jan Maarten van Dijl
TatAc, the third TatA subunit of Bacillus subtilis, can form active twin-arginine translocases with the TatCd and TatCy subunits.
Appl Environ Microbiol: 2012, 78(14);4999-5001
[PubMed:22544248]
[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)
Olga V Nolandt, Torsten H Walther, Siegmar Roth, Jochen Bürck, Anne S Ulrich
Structure analysis of the membrane protein TatC(d) from the Tat system of B. subtilis by circular dichroism.
Biochim Biophys Acta: 2009, 1788(10);2238-44
[PubMed:19616508]
[WorldCat.org]
[DOI]
(P p)
Anja N J A Ridder, Esther J de Jong, Jan D H Jongbloed, Oscar P Kuipers
Subcellular localization of TatAd of Bacillus subtilis depends on the presence of TatCd or TatCy.
J Bacteriol: 2009, 191(13);4410-8
[PubMed:19395490]
[WorldCat.org]
[DOI]
(I p)
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)
J D Jongbloed, U Martin, H Antelmann, M Hecker, H Tjalsma, G Venema, S Bron, J M van Dijl, J Müller
TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway.
J Biol Chem: 2000, 275(52);41350-7
[PubMed:11007775]
[WorldCat.org]
[DOI]
(P p)
S Eder, W Liu, F M Hulett
Mutational analysis of the phoD promoter in Bacillus subtilis: implications for PhoP binding and promoter activation of Pho regulon promoters.
J Bacteriol: 1999, 181(7);2017-25
[PubMed:10094677]
[WorldCat.org]
[DOI]
(P p)