ComFA

• Description: membrane-associated ATPase, may provide energy for DNA transport
  
  

Gene name	comFA
Synonyms
Essential	no
Product	ATP-binding protein
Function	genetic competence
Gene expression levels in SubtiExpress: comFA
Interactions involving this protein in SubtInteract: ComFA
Metabolic function and regulation of this protein in SubtiPathways: ComFA
MW, pI	52 kDa, 9.824
Gene length, protein length	1389 bp, 463 aa
Immediate neighbours	comFB, yviA
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

genetic competence, membrane proteins, phosphoproteins

This gene is a member of the following regulons

ComK regulon

The gene

Basic information

• Locus tag: BSU35470

Database entries

• BsubCyc: BSU35470

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

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

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-20, Arg-186, and Arg-446 PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • ComGA-ComFA PubMed
  • ComEC-ComFA PubMed
  • CoiA-ComFA PubMed
  • SsbB-ComFA PubMed
  • DprA-ComFA PubMed
  • RecA-ComFA PubMed

• Localization:
  • cell membrane PubMed
  • localizes to cell poles in competent cells PubMed
  • localizes to cell poles PubMed

Database entries

• BsubCyc: BSU35470

• Structure:

• UniProt: P39145

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: comFA-comFB-comFC-yvyF-flgM-yvyG-flgK-flgL PubMed

• Expression browser: comFA PubMed

• Sigma factor: comFA: SigA PubMed

• Regulation:

• Regulatory mechanism:
  • ComK: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Inês Chen, David Dubnau
DNA uptake during bacterial transformation.
Nat Rev Microbiol: 2004, 2(3);241-9
[PubMed:15083159] [WorldCat.org] [DOI] (P p)

Original publications

Additional publications: PubMed

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Miriam Kaufenstein, Martin van der Laan, Peter L Graumann
The three-layered DNA uptake machinery at the cell pole in competent Bacillus subtilis cells is a stable complex.
J Bacteriol: 2011, 193(7);1633-42
[PubMed:21278288] [WorldCat.org] [DOI] (I p)

Naomi Kramer, Jeanette Hahn, David Dubnau
Multiple interactions among the competence proteins of Bacillus subtilis.
Mol Microbiol: 2007, 65(2);454-64
[PubMed:17630974] [WorldCat.org] [DOI] (P p)

Jeanette Hahn, Berenike Maier, Bert Jan Haijema, Michael Sheetz, David Dubnau
Transformation proteins and DNA uptake localize to the cell poles in Bacillus subtilis.
Cell: 2005, 122(1);59-71
[PubMed:16009133] [WorldCat.org] [DOI] (P p)

Hanne Jarmer, Randy Berka, Steen Knudsen, Hans H Saxild
Transcriptome analysis documents induced competence of Bacillus subtilis during nitrogen limiting conditions.
FEMS Microbiol Lett: 2002, 206(2);197-200
[PubMed:11814663] [WorldCat.org] [DOI] (P p)

J A Londoño-Vallejo, D Dubnau
Mutation of the putative nucleotide binding site of the Bacillus subtilis membrane protein ComFA abolishes the uptake of DNA during transformation.
J Bacteriol: 1994, 176(15);4642-5
[PubMed:8045895] [WorldCat.org] [DOI] (P p)

J A Londoño-Vallejo, D Dubnau
Membrane association and role in DNA uptake of the Bacillus subtilis PriA analogue ComF1.
Mol Microbiol: 1994, 13(2);197-205
[PubMed:7984101] [WorldCat.org] [DOI] (P p)

J A Londoño-Vallejo, D Dubnau
comF, a Bacillus subtilis late competence locus, encodes a protein similar to ATP-dependent RNA/DNA helicases.
Mol Microbiol: 1993, 9(1);119-31
[PubMed:8412657] [WorldCat.org] [DOI] (P p)