SipT

• Description: signal peptidase I
  
  

Gene name	sipT
Synonyms
Essential	no
Product	signal peptidase I
Function	protein secretion
MW, pI	21 kDa, 9.851
Gene length, protein length	579 bp, 193 aa
Immediate neighbours	fruA, ykoA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU14410

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

Categories containing this gene/protein

protein secretion, membrane proteins

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, SipU, 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: P71013

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: sipT PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:
  • DegU: transcription activation PubMed

• 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

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)