FabF

• Description: beta-ketoacyl-acyl carrier protein synthase II, involved in the control of membrane fluidity
  
  

Gene name	fabF
Synonyms	yjaY
Essential	yes PubMed
Product	beta-ketoacyl-acyl carrier protein synthase II
Function	fatty acid biosynthesis
Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis
MW, pI	43 kDa, 4.768
Gene length, protein length	1239 bp, 413 aa
Immediate neighbours	fabHA, yjaZ
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

biosynthesis of lipids, cell envelope stress proteins (controlled by SigM, V, W, X, Y), essential genes

This gene is a member of the following regulons

FapR regulon, SigW regulon

The gene

Basic information

• Locus tag: BSU11340

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO₂ + [acyl-carrier-protein] (according to Swiss-Prot)
  • SigW-dependent expression of fabF and the yuaF-floT-yuaI operon result in reduced membrane fluidity PubMed

• Protein family: beta-ketoacyl-ACP synthases family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1OX0 (the protein from Streptococcus pneumoniae) PubMed

• UniProt: O34340

• KEGG entry: [3]

• E.C. number: 2.3.1.179

Expression and regulation

• Operon: fabHA-fabF PubMed

• Sigma factor:
  • fabHA: SigA PubMed
  • fabF: SigW PubMed

• Regulation:
  • fabHA: expressed when the cells experience a lack of malonyl-CoA (FapR) PubMed
  • fabHA: induced upon fatty acid biosynthesis inhibition PubMed
  • fabF: induced by alkaline shock and by polymyxin B, vancomycin, cephalosporin C, D-cycloserine, and triton X-100 (SigW) PubMed

• Regulatory mechanism:
  • FapR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Yasutaro Fujita, Hiroshi Matsuoka, Kazutake Hirooka
Regulation of fatty acid metabolism in bacteria.
Mol Microbiol: 2007, 66(4);829-39
[PubMed:17919287] [WorldCat.org] [DOI] (P p)

Stephen W White, Jie Zheng, Yong-Mei Zhang, Rock
The structural biology of type II fatty acid biosynthesis.
Annu Rev Biochem: 2005, 74;791-831
[PubMed:15952903] [WorldCat.org] [DOI] (P p)

Original Publications

Additional publications: PubMed

Michaela Wenzel, Malay Patra, Dirk Albrecht, David Y-K Chen, K C Nicolaou, Nils Metzler-Nolte, Julia E Bandow
Proteomic signature of fatty acid biosynthesis inhibition available for in vivo mechanism-of-action studies.
Antimicrob Agents Chemother: 2011, 55(6);2590-6
[PubMed:21383089] [WorldCat.org] [DOI] (I p)

Gustavo E Schujman, Silvia Altabe, Diego de Mendoza
A malonyl-CoA-dependent switch in the bacterial response to a dysfunction of lipid metabolism.
Mol Microbiol: 2008, 68(4);987-96
[PubMed:18384517] [WorldCat.org] [DOI] (I p)

Allen C Price, Charles O Rock, Stephen W White
The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae.
J Bacteriol: 2003, 185(14);4136-43
[PubMed:12837788] [WorldCat.org] [DOI] (P p)

Gustavo E Schujman, Luciana Paoletti, Alan D Grossman, Diego de Mendoza
FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis.
Dev Cell: 2003, 4(5);663-72
[PubMed:12737802] [WorldCat.org] [DOI] (P p)

K Kobayashi, S D Ehrlich, A Albertini, G Amati, K K Andersen, M Arnaud, K Asai, S Ashikaga, S Aymerich, P Bessieres, F Boland, S C Brignell, S Bron, K Bunai, J Chapuis, L C Christiansen, A Danchin, M Débarbouille, E Dervyn, E Deuerling, K Devine, S K Devine, O Dreesen, J Errington, S Fillinger, S J Foster, Y Fujita, A Galizzi, R Gardan, C Eschevins, T Fukushima, K Haga, C R Harwood, M Hecker, D Hosoya, M F Hullo, H Kakeshita, D Karamata, Y Kasahara, F Kawamura, K Koga, P Koski, R Kuwana, D Imamura, M Ishimaru, S Ishikawa, I Ishio, D Le Coq, A Masson, C Mauël, R Meima, R P Mellado, A Moir, S Moriya, E Nagakawa, H Nanamiya, S Nakai, P Nygaard, M Ogura, T Ohanan, M O'Reilly, M O'Rourke, Z Pragai, H M Pooley, G Rapoport, J P Rawlins, L A Rivas, C Rivolta, A Sadaie, Y Sadaie, M Sarvas, T Sato, H H Saxild, E Scanlan, W Schumann, J F M L Seegers, J Sekiguchi, A Sekowska, S J Séror, M Simon, P Stragier, R Studer, H Takamatsu, T Tanaka, M Takeuchi, H B Thomaides, V Vagner, J M van Dijl, K Watabe, A Wipat, H Yamamoto, M Yamamoto, Y Yamamoto, K Yamane, K Yata, K Yoshida, H Yoshikawa, U Zuber, N Ogasawara
Essential Bacillus subtilis genes.
Proc Natl Acad Sci U S A: 2003, 100(8);4678-83
[PubMed:12682299] [WorldCat.org] [DOI] (P p)