Maf

• Description: cell division inhibitor in competent cells, blocks septation during the escape from competence, required for the stability of ComGA
  
  

Gene name	maf
Synonyms
Essential	no
Product	cell division inhibitor
Function	cell division control
Gene expression levels in SubtiExpress: maf
Interactions involving this protein in SubtInteract: Maf
MW, pI	21 kDa, 5.711
Gene length, protein length	567 bp, 189 aa
Immediate neighbours	radC, spoIIB
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell division, genetic competence

This gene is a member of the following regulons

ComK regulon

The gene

Basic information

• Locus tag: BSU28050

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: maf family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors: binds phosphorylated compounds (UTP, IMP, IDP, GDP and others) in in vitro experiments

• Effectors of protein activity:

• Interactions:
  • forms dimers PubMed
  • Maf-DivIVA PubMed
  • Maf-FtsW PubMed
  • Maf-ComGA PubMed

• Localization:
  • cytosolic protein PubMed
  • near the poles of competent cells PubMed

Database entries

• Structure: 1EX2

• UniProt: Q02169

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: maf PubMed

• Sigma factor:

• Regulation:
  • expressed when cells enter the compentent state (ComK) PubMed
  • expression is reduced in a SigV mutant PubMed

• Regulatory mechanism:
  • ComK: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Leendert W Hamoen
Cell division blockage: but this time by a surprisingly conserved protein.
Mol Microbiol: 2011, 81(1);1-3
[PubMed:21595759] [WorldCat.org] [DOI] (I p)

Original publications

Jessica M Mann, Valerie J Carabetta, Ileana M Cristea, David Dubnau
Complex formation and processing of the minor transformation pilins of Bacillus subtilis.
Mol Microbiol: 2013, 90(6);1201-15
[PubMed:24164455] [WorldCat.org] [DOI] (I p)

Veronica Guariglia-Oropeza, John D Helmann
Bacillus subtilis σ(V) confers lysozyme resistance by activation of two cell wall modification pathways, peptidoglycan O-acetylation and D-alanylation of teichoic acids.
J Bacteriol: 2011, 193(22);6223-32
[PubMed:21926231] [WorldCat.org] [DOI] (I p)

Kenneth Briley, Peter Prepiak, Miguel J Dias, Jeanette Hahn, David Dubnau
Maf acts downstream of ComGA to arrest cell division in competent cells of B. subtilis.
Mol Microbiol: 2011, 81(1);23-39
[PubMed:21564336] [WorldCat.org] [DOI] (I p)

Mitsuo Ogura, Hirotake Yamaguchi, Kazuo Kobayashi, Naotake Ogasawara, Yasutaro Fujita, Teruo Tanaka
Whole-genome analysis of genes regulated by the Bacillus subtilis competence transcription factor ComK.
J Bacteriol: 2002, 184(9);2344-51
[PubMed:11948146] [WorldCat.org] [DOI] (P p)

G Minasov, M Teplova, G C Stewart, E V Koonin, W F Anderson, M Egli
Functional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTP.
Proc Natl Acad Sci U S A: 2000, 97(12);6328-33
[PubMed:10841541] [WorldCat.org] [DOI] (P p)

Y X Butler, Y Abhayawardhane, G C Stewart
Amplification of the Bacillus subtilis maf gene results in arrested septum formation.
J Bacteriol: 1993, 175(10);3139-45
[PubMed:8387996] [WorldCat.org] [DOI] (P p)