Difference between revisions of "SpoIVB"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[spo0A]]'', ''[[recN]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[spo0A]]'', ''[[recN]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU24230 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU24230 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU24230 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU24230 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU24230 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU24230 DNA_with_flanks]
 
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Revision as of 10:41, 14 May 2013

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

Gene name spoIVB
Synonyms
Essential no
Product serine protease
Function control of SigK activation
Gene expression levels in SubtiExpress: spoIVB
Interactions involving this protein in SubtInteract: SpoIVB
MW, pI 45 kDa, 8.842
Gene length, protein length 1275 bp, 425 aa
Immediate neighbours spo0A, recN
Sequences Protein DNA DNA_with_flanks
Genetic context
SpoIVB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SpoIVB expression.png
























Categories containing this gene/protein

sigma factors and their control, sporulation proteins

This gene is a member of the following regulons

SigF regulon, SigG regulon

The gene

Basic information

  • Locus tag: BSU24230

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and 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

Your additional remarks

References

Nathalie Campo, David Z Rudner
SpoIVB and CtpB are both forespore signals in the activation of the sporulation transcription factor sigmaK in Bacillus subtilis.
J Bacteriol: 2007, 189(16);6021-7
[PubMed:17557826] [WorldCat.org] [DOI] (P p)

Thierry Doan, David Z Rudner
Perturbations to engulfment trigger a degradative response that prevents cell-cell signalling during sporulation in Bacillus subtilis.
Mol Microbiol: 2007, 64(2);500-11
[PubMed:17493131] [WorldCat.org] [DOI] (P p)

Nathalie Campo, David Z Rudner
A branched pathway governing the activation of a developmental transcription factor by regulated intramembrane proteolysis.
Mol Cell: 2006, 23(1);25-35
[PubMed:16818230] [WorldCat.org] [DOI] (P p)

Stephanie T Wang, Barbara Setlow, Erin M Conlon, Jessica L Lyon, Daisuke Imamura, Tsutomu Sato, Peter Setlow, Richard Losick, Patrick Eichenberger
The forespore line of gene expression in Bacillus subtilis.
J Mol Biol: 2006, 358(1);16-37
[PubMed:16497325] [WorldCat.org] [DOI] (P p)

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)

Qi Pan, Richard Losick, David Z Rudner
A second PDZ-containing serine protease contributes to activation of the sporulation transcription factor sigmaK in Bacillus subtilis.
J Bacteriol: 2003, 185(20);6051-6
[PubMed:14526016] [WorldCat.org] [DOI] (P p)

Tran C Dong, Simon M Cutting
SpoIVB-mediated cleavage of SpoIVFA could provide the intercellular signal to activate processing of Pro-sigmaK in Bacillus subtilis.
Mol Microbiol: 2003, 49(5);1425-34
[PubMed:12940997] [WorldCat.org] [DOI] (P p)

Ngo T Hoa, James A Brannigan, Simon M Cutting
The Bacillus subtilis signaling protein SpoIVB defines a new family of serine peptidases.
J Bacteriol: 2002, 184(1);191-9
[PubMed:11741860] [WorldCat.org] [DOI] (P p)

N T Hoa, J A Brannigan, S M Cutting
The PDZ domain of the SpoIVB serine peptidase facilitates multiple functions.
J Bacteriol: 2001, 183(14);4364-73
[PubMed:11418578] [WorldCat.org] [DOI] (P p)

P Wakeley, N T Hoa, S Cutting
BofC negatively regulates SpoIVB-mediated signalling in the Bacillus subtilis sigmaK-checkpoint.
Mol Microbiol: 2000, 36(6);1415-24
[PubMed:10931291] [WorldCat.org] [DOI] (P p)

P R Wakeley, R Dorazi, N T Hoa, J R Bowyer, S M Cutting
Proteolysis of SpolVB is a critical determinant in signalling of Pro-sigmaK processing in Bacillus subtilis.
Mol Microbiol: 2000, 36(6);1336-48
[PubMed:10931284] [WorldCat.org] [DOI] (P p)

M Gomez, S M Cutting
Expression of the Bacillus subtilis spoIVB gene is under dual sigma F/sigma G control.
Microbiology (Reading): 1996, 142 ( Pt 12);3453-7
[PubMed:9004507] [WorldCat.org] [DOI] (P p)

I Bagyan, J Hobot, S Cutting
A compartmentalized regulator of developmental gene expression in Bacillus subtilis.
J Bacteriol: 1996, 178(15);4500-7
[PubMed:8755877] [WorldCat.org] [DOI] (P p)

S Cutting, A Driks, R Schmidt, B Kunkel, R Losick
Forespore-specific transcription of a gene in the signal transduction pathway that governs Pro-sigma K processing in Bacillus subtilis.
Genes Dev: 1991, 5(3);456-66
[PubMed:1900494] [WorldCat.org] [DOI] (P p)

B E Van Hoy, J A Hoch
Characterization of the spoIVB and recN loci of Bacillus subtilis.
J Bacteriol: 1990, 172(3);1306-11
[PubMed:2106508] [WorldCat.org] [DOI] (P p)