Difference between revisions of "FabF"

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(Database entries)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1OX0 1OX0] (the protein from ''Streptococcus pneumoniae'') {{PubMed|12837788}}  
+
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=4LS5 4LS5] {{PubMed|24641521}}  
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34340 O34340]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34340 O34340]

Revision as of 09:46, 20 March 2014

  • 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
Gene expression levels in SubtiExpress: fabF
Metabolic function and regulation of this protein in SubtiPathways:
fabF
MW, pI 43 kDa, 4.768
Gene length, protein length 1239 bp, 413 aa
Immediate neighbours fabHA, yjaZ
Sequences Protein DNA DNA_with_flanks
Genetic context
FabF context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FabF expression.png















Categories containing this gene/protein

membrane dynamics, 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]

Additional information

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:
  • Modification:
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

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

Felipe Trajtenberg, Silvia Altabe, Nicole Larrieux, Florencia Ficarra, Diego de Mendoza, Alejandro Buschiazzo, Gustavo E Schujman
Structural insights into bacterial resistance to cerulenin.
FEBS J: 2014, 281(10);2324-38
[PubMed:24641521] [WorldCat.org] [DOI] (I p)

Yong Heon Lee, Anthony W Kingston, John D Helmann
Glutamate dehydrogenase affects resistance to cell wall antibiotics in Bacillus subtilis.
J Bacteriol: 2012, 194(5);993-1001
[PubMed:22178969] [WorldCat.org] [DOI] (I p)

Anthony W Kingston, Chitra Subramanian, Charles O Rock, John D Helmann
A σW-dependent stress response in Bacillus subtilis that reduces membrane fluidity.
Mol Microbiol: 2011, 81(1);69-79
[PubMed:21542858] [WorldCat.org] [DOI] (I p)

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)