SpoIVB

• Description: serine protease, cleaves SpoIVFA, this results in pro-sigma-K processing/activation in the mother-cell, does also cleave CtpB
  
  

Gene name	spoIVB
Synonyms
Essential	no
Product	serine protease
Function	control of SigK activation
MW, pI	45 kDa, 8.842
Gene length, protein length	1275 bp, 425 aa
Immediate neighbours	spo0A, recN
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: BSU24230

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Self-cleaves 52-Val-|-Asn-53, 62-Ala-|-Phe-63 and 74-Val-|-Thr-75 at the N-terminus of SpoIVB (according to Swiss-Prot)

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: SpoIVB-BofA PubMed, BofC-SpoIVB PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure:

• Swiss prot entry: P17896

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:

• 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

Simon Cutting, London, UK homepage

References

Tran C Dong, Simon M Cutting
The PDZ domain of the SpoIVB transmembrane signaling protein enables cis-trans interactions involving multiple partners leading to the activation of the pro-sigmaK processing complex in Bacillus subtilis.
J Biol Chem: 2004, 279(42);43468-78
[PubMed:15292188] [WorldCat.org] [DOI] (P p)

1. Dong & Cutting (2004) The PDZ domain of the SpoIVB transmembrane signaling protein enables cis-trans interactions involving multiple partners leading to the activation of the pro-sigmaK processing complex in Bacillus subtilis.J. Biol. Chem. 279: 43468-43478. PubMed
2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed