Difference between revisions of "FabL"

From SubtiWiki
Jump to: navigation, search
Line 129: Line 129:
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 206 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 206 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 750 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 750 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1540 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1009 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1634 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:06, 17 April 2014

  • Description: enoyl-acyl carrier protein reductase

Gene name fabL
Synonyms yfhR, ygaA
Essential no
Product enoyl-acyl carrier protein reductase
Function fatty acid biosynthesis
Gene expression levels in SubtiExpress: fabL
Metabolic function and regulation of this protein in SubtiPathways:
fabL
MW, pI 27 kDa, 5.967
Gene length, protein length 750 bp, 250 aa
Immediate neighbours yfhS, sspE
Sequences Protein DNA DNA_with_flanks
Genetic context
FabL context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FabL expression.png




























Categories containing this gene/protein

biosynthesis of lipids, sporulation proteins

This gene is a member of the following regulons

SigG regulon, SpoVT regulon, YfhP regulon

The gene

Basic information

  • Locus tag: BSU08650

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s): FabI, one of the two proteins has to be present for viability PubMed

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 206 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 750 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1540 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1009 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1634 PubMed

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

Kook-Han Kim, Byung Hak Ha, Su Jin Kim, Seung Kon Hong, Kwang Yeon Hwang, Eunice Eunkyeong Kim
Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis.
J Mol Biol: 2011, 406(3);403-15
[PubMed:21185310] [WorldCat.org] [DOI] (I p)

Helena B Thomaides, Ella J Davison, Lisa Burston, Hazel Johnson, David R Brown, Alison C Hunt, Jeffery Errington, Lloyd Czaplewski
Essential bacterial functions encoded by gene pairs.
J Bacteriol: 2007, 189(2);591-602
[PubMed:17114254] [WorldCat.org] [DOI] (P p)

Leif Steil, Mónica Serrano, Adriano O Henriques, Uwe Völker
Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis.
Microbiology (Reading): 2005, 151(Pt 2);399-420
[PubMed:15699190] [WorldCat.org] [DOI] (P p)

R J Heath, N Su, C K Murphy, C O Rock
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis.
J Biol Chem: 2000, 275(51);40128-33
[PubMed:11007778] [WorldCat.org] [DOI] (P p)

Hiroki Yamamoto, Masao Mori, Junichi Sekiguchi
Transcription of genes near the sspE locus of the Bacillus subtilis genome.
Microbiology (Reading): 1999, 145 ( Pt 8);2171-2180
[PubMed:10463184] [WorldCat.org] [DOI] (P p)

I Bagyan, J Hobot, S Cutting
A compartmentalized regulator of developmental gene expression in Bacillus subtilis.
J Bacteriol: 1996, 178(15);4500-7
[PubMed:8755877] [WorldCat.org] [DOI] (P p)