SipU

• Description: signal peptidase I
  
  

Gene name	sipU
Synonyms	ycsB
Essential	no
Product	signal peptidase I
Function	protein secretion
Gene expression levels in SubtiExpress: sipU
Metabolic function and regulation of this protein in SubtiPathways: Protein secretion
MW, pI	21 kDa, 9.844
Gene length, protein length	561 bp, 187 aa
Immediate neighbours	ycsA, yczH
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

protein secretion, membrane proteins

The gene

Basic information

• Locus tag: BSU04010

Database entries

• 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): SipS, SipT, SipV

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: P42959

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: sipU (according to DBTBS)

• Expression browser: sipU PubMed

• Sigma factor:

• 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

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

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)