LutA

• Description: lactate catabolic enzyme
  
  

Gene name	lutA
Synonyms	yvfV
Essential	no
Product	lactate oxidase
Function	lactate utilization
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	26 kDa, 6.25
Gene length, protein length	714 bp, 238 aa
Immediate neighbours	lutB, yvfU
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

LutR regulon, SinR regulon

The gene

Basic information

• Locus tag: BSU34050

Phenotypes of a mutant

no growth with lactate as the single carbon source PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: oxidation of lactate to pyruvate PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: O07020

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: lutA-lutB-lutC PubMed

• Sigma factor:

• Regulation: induction by lactate PubMed
  • repressed by SinR PubMed
  • part of the iron sparing response, down-regulation in a fur mutant (Fur, FsrA, FpbB) PubMed

• Regulatory mechanism: dual repression by LutR (inducer lactate) and SinR PubMed
  • SinR: transcription repression PubMed
  • FsrA: translational repression PubMed
  • FbpB: acts as RNA chaperone, increases interaction between fsrA and lutA-lutB-lutC RNAs PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Richard Losick, Harvard Univ., Cambridge, USA homepage

References

Gregory T Smaldone, Haike Antelmann, Ahmed Gaballa, John D Helmann
The FsrA sRNA and FbpB protein mediate the iron-dependent induction of the Bacillus subtilis lutABC iron-sulfur-containing oxidases.
J Bacteriol: 2012, 194(10);2586-93
[PubMed:22427629] [WorldCat.org] [DOI] (I p)

Yunrong Chai, Roberto Kolter, Richard Losick
A widely conserved gene cluster required for lactate utilization in Bacillus subtilis and its involvement in biofilm formation.
J Bacteriol: 2009, 191(8);2423-30
[PubMed:19201793] [WorldCat.org] [DOI] (I p)

Frances Chu, Daniel B Kearns, Steven S Branda, Roberto Kolter, Richard Losick
Targets of the master regulator of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2006, 59(4);1216-28
[PubMed:16430695] [WorldCat.org] [DOI] (P p)