Difference between revisions of "SipT"

From SubtiWiki
Jump to: navigation, search
Line 119: Line 119:
  
 
* '''Additional information:'''
 
* '''Additional information:'''
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium): 45 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 10:02, 17 April 2014

  • 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:
SipT
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:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 45 PubMed

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)