AcoL

• Description: acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase)
  
  

Gene name	acoL
Synonyms	yfjH
Essential	no
Product	acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase)
Function	acetoin utilization
Interactions involving this protein in SubtInteract: AcoL
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	48 kDa, 5.273
Gene length, protein length	1374 bp, 458 aa
Immediate neighbours	acoC, acoR
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

AcoR regulon, CcpA regulon, SigL regulon

The gene

Basic information

• Locus tag: BSU08090

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Protein N(6)-(dihydrolipoyl)lysine + NAD⁺ = protein N(6)-(lipoyl)lysine + NADH (according to Swiss-Prot)

• Protein family: class-I pyridine nucleotide-disulfide oxidoreductase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • (AcoA-AcoB)-AcoC-AcoL

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: O34324

• KEGG entry: [3]

• E.C. number: 1.8.1.4

Expression and regulation

• Operon: acoA-acoB-acoC-acoL PubMed

• Sigma factor: SigL PubMed

• Regulation:
  • repressed by glucose (CcpA) PubMed
  • induced by acetoin (AcoR) PubMed
  • induced under anaerobic conditions (Fnr) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • AcoR: transcription activation (interaction with SigL-containing RNA polymerase) PubMed
  • Fnr: indirect positive regulation via NarG-NarH-NarJ-NarI PubMed

• Additional information:
  • the mRNA is very stable (half-life > 15 min) PubMed
  • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Michel Debarbouille, Pasteur Institute, Paris, France Homepage

References

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947

Heike Reents, Richard Münch, Thorben Dammeyer, Dieter Jahn, Elisabeth Härtig
The Fnr regulon of Bacillus subtilis.
J Bacteriol: 2006, 188(3);1103-12
[PubMed:16428414] [WorldCat.org] [DOI] (P p)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [WorldCat.org] [DOI] (P p)

N O Ali, J Bignon, G Rapoport, M Debarbouille
Regulation of the acetoin catabolic pathway is controlled by sigma L in Bacillus subtilis.
J Bacteriol: 2001, 183(8);2497-504
[PubMed:11274109] [WorldCat.org] [DOI] (P p)

Y Miwa, A Nakata, A Ogiwara, M Yamamoto, Y Fujita
Evaluation and characterization of catabolite-responsive elements (cre) of Bacillus subtilis.
Nucleic Acids Res: 2000, 28(5);1206-10
[PubMed:10666464] [WorldCat.org] [DOI] (I p)

M Huang, F B Oppermann-Sanio, A Steinbüchel
Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway.
J Bacteriol: 1999, 181(12);3837-41
[PubMed:10368162] [WorldCat.org] [DOI] (P p)