Difference between revisions of "SipS"
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* '''Operon:''' ''sipS'' {{PubMed|8951809}} | * '''Operon:''' ''sipS'' {{PubMed|8951809}} | ||
− | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sipS_2432316_2432870_-1 sipS] {{PubMed|22383849}} |
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+ | * '''Sigma factor:''' [[SigA]] {{PubMed|8951809}} | ||
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | * '''Additional information:''' | + | * '''Additional information:''' |
=Biological materials = | =Biological materials = |
Revision as of 10:28, 16 April 2012
- 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 This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
protein secretion, membrane proteins
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:
- Localization: membrane
Database entries
- Structure:
- UniProt: P28628
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: sipS PubMed
- 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)