Difference between revisions of "SipS"

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|style="background:#ABCDEF;" align="center"|'''Function''' || protein secretion
 
|style="background:#ABCDEF;" align="center"|'''Function''' || protein secretion
 
(modulation of the capacity and specificity for protein secretion)
 
(modulation of the capacity and specificity for protein secretion)
 +
|-
 +
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 20 kDa, 9.718   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 20 kDa, 9.718   

Revision as of 13:45, 11 December 2010

  • Description: signal peptidase I

Gene name sipS
Synonyms
Essential no
Product signal peptidase I
Function protein secretion

(modulation of the capacity and specificity for protein secretion)

Metabolic function and regulation of this protein in SubtiPathways:
Protein secretion
MW, pI 20 kDa, 9.718
Gene length, protein length 552 bp, 184 aa
Immediate neighbours ypuD, ypzC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SipS context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

protein secretion

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU23310

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:
  • Interactions:
  • Localization:

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

A Bolhuis, H Tjalsma, K Stephenson, C R Harwood, G Venema, S Bron, J M van Dijl
Different mechanisms for thermal inactivation of Bacillus subtilis signal peptidase mutants.
J Biol Chem: 1999, 274(22);15865-8
[PubMed:10336490] [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)

A Bolhuis, A Sorokin, V Azevedo, S D Ehrlich, P G Braun, A de Jong, G Venema, S Bron, J M van Dijl
Bacillus subtilis can modulate its capacity and specificity for protein secretion through temporally controlled expression of the sipS gene for signal peptidase I.
Mol Microbiol: 1996, 22(4);605-18
[PubMed:8951809] [WorldCat.org] [DOI] (P p)