Difference between revisions of "SipT"

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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sipT_1511308_1511889_1 sipT] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sipT_1511308_1511889_1 sipT] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
 
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== Reviews ==
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<pubmed>22688815 </pubmed>
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== Original publications ==
 
<pubmed>11807061,9325333,9694797,, </pubmed>
 
<pubmed>11807061,9325333,9694797,, </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:38, 31 July 2013

  • Description: signal peptidase I

Gene name sipT
Synonyms
Essential no
Product signal peptidase I
Function protein secretion
Gene expression levels in SubtiExpress: sipT
Metabolic function and regulation of this protein in SubtiPathways:
Protein secretion
MW, pI 21 kDa, 9.851
Gene length, protein length 579 bp, 193 aa
Immediate neighbours fruA, ykoA
Sequences Protein DNA DNA_with_flanks
Genetic context
SipT context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SipT expression.png















Categories containing this gene/protein

protein secretion, membrane proteins

This gene is a member of the following regulons

DegU regulon

The gene

Basic information

  • Locus tag: BSU14410

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins (according to Swiss-Prot)
  • Protein family: peptidase S26 family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Jan Maarten van Dijl, Groningen, Netherlands

Your additional remarks

References

Reviews

Ross E Dalbey, Peng Wang, Jan Maarten van Dijl
Membrane proteases in the bacterial protein secretion and quality control pathway.
Microbiol Mol Biol Rev: 2012, 76(2);311-30
[PubMed:22688815] [WorldCat.org] [DOI] (I p)

Original publications

Tiina Pummi, Soile Leskelä, Eva Wahlström, Ulf Gerth, Harold Tjalsma, Michael Hecker, Matti Sarvas, Vesa P Kontinen
ClpXP protease regulates the signal peptide cleavage of secretory preproteins in Bacillus subtilis with a mechanism distinct from that of the Ecs ABC transporter.
J Bacteriol: 2002, 184(4);1010-8
[PubMed:11807061] [WorldCat.org] [DOI] (P p)

H Tjalsma, A Bolhuis, M L van Roosmalen, T Wiegert, W Schumann, C P Broekhuizen, W J Quax, G Venema, S Bron, J M van Dijl
Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases.
Genes Dev: 1998, 12(15);2318-31
[PubMed:9694797] [WorldCat.org] [DOI] (P p)

H Tjalsma, M A Noback, S Bron, G Venema, K Yamane, J M van Dijl
Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities. Constitutive and temporally controlled expression of different sip genes.
J Biol Chem: 1997, 272(41);25983-92
[PubMed:9325333] [WorldCat.org] [DOI] (P p)