SipS

• 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)
Gene expression levels in SubtiExpress: sipS (modulation of the capacity and specificity for protein secretion)
Metabolic function and regulation of this protein in SubtiPathways: SipS
MW, pI	20 kDa, 9.718
Gene length, protein length	552 bp, 184 aa
Immediate neighbours	ypuD, ypzC
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed 500px

Categories containing this gene/protein

protein secretion, membrane proteins

The gene

Basic information

• Locus tag: BSU23310

Phenotypes of a mutant

• • a sipS sipT double mutant is not viable PubMed

Database entries

• BsubCyc: BSU23310

• DBTBS entry: [1]

• SubtiList entry: [2]

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)

• Paralogous protein(s): SipT, SipU, SipV

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: membrane

Database entries

• BsubCyc: BSU23310

• Structure:

• UniProt: P28628

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: sipS PubMed

• Expression browser: sipS PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 129 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 363 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

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

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)