BofA

• Description: inhibition of the pro-sigma-K processing machinery
  
  

Gene name	bofA
Synonyms
Essential	no
Product	inhibitor of pro-SigK processing
Function	control of SigK activation
Interactions involving this protein in SubtInteract: BofA
MW, pI	8 kDa, 9.32
Gene length, protein length	261 bp, 87 aa
Immediate neighbours	yaaL, rrnA-16S
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

sigma factors and their control, sporulation proteins, membrane proteins

This gene is a member of the following regulons

SigE regulon, SpoIIID regulon

The gene

Basic information

• Locus tag: BSU00230

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • BofA-SpoIVB PubMed

• Localization: forespore outer membrane (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: P24282

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: bofA PubMed

• Sigma factor: SigE PubMed

• Regulation: expressed during sporulation PubMed

• Regulatory mechanism: repressed by SpoIIID PubMed

• Additional information: the mRNA is very stable (half-life > 15 min) PubMed

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

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)

Thierry Doan, Kathleen A Marquis, David Z Rudner
Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum.
Mol Microbiol: 2005, 55(6);1767-81
[PubMed:15752199] [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)

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)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [WorldCat.org] [DOI] (P p)

David Z Rudner, Richard Losick
A sporulation membrane protein tethers the pro-sigmaK processing enzyme to its inhibitor and dictates its subcellular localization.
Genes Dev: 2002, 16(8);1007-18
[PubMed:11959848] [WorldCat.org] [DOI] (P p)

O Resnekov, R Losick
Negative regulation of the proteolytic activation of a developmental transcription factor in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1998, 95(6);3162-7
[PubMed:9501233] [WorldCat.org] [DOI] (P p)

E Ricca, S Cutting, R Losick
Characterization of bofA, a gene involved in intercompartmental regulation of pro-sigma K processing during sporulation in Bacillus subtilis.
J Bacteriol: 1992, 174(10);3177-84
[PubMed:1577688] [WorldCat.org] [DOI] (P p)

K Ireton, A D Grossman
Interactions among mutations that cause altered timing of gene expression during sporulation in Bacillus subtilis.
J Bacteriol: 1992, 174(10);3185-95
[PubMed:1315731] [WorldCat.org] [DOI] (P p)

S Cutting, V Oke, A Driks, R Losick, S Lu, L Kroos
A forespore checkpoint for mother cell gene expression during development in B. subtilis.
Cell: 1990, 62(2);239-50
[PubMed:2115401] [WorldCat.org] [DOI] (P p)