TatCY

• Description: component of the TatAY-TatCY twin-arginine translocase
  
  

Gene name	tatCY
Synonyms	ydiJ
Essential	no
Product	component of the twin-arginine translocation pathway
Function	TAT protein secretion
Gene expression levels in SubtiExpress: tatCY
Interactions involving this protein in SubtInteract: TatCY
Metabolic function and regulation of this protein in SubtiPathways: Protein secretion
MW, pI	28 kDa, 9.685
Gene length, protein length	762 bp, 254 aa
Immediate neighbours	tatAY, ydiK
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

protein secretion, membrane proteins

The gene

Basic information

• Locus tag: BSU05990

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: secretion of YwbN and YkuE

• Protein family: tatC family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • TatAY-TatCY PubMed
  • TatAD-TatCY PubMed
  • TatAC-TatCY PubMed

• Localization: cell membrane (according to Swiss-Prot), Polar (Septum) PubMed

Database entries

• Structure:

• UniProt: O05523

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:
  • ydiG-rex-tatAY-tatCY PubMed
  • tatAY-tatCY PubMed

• Expression browser: tatCY PubMed

• Sigma factor:

• Regulation: constitutitvely expressed PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

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

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)

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)

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)

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)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [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)