LutA

• Description: lactate catabolic enzyme
  
  

Gene name	lutA
Synonyms	yvfV
Essential	no
Product	lactate oxidase
Function	lactate utilization
Gene expression levels in SubtiExpress: lutA
Metabolic function and regulation of this protein in SubtiPathways: lutA
MW, pI	26 kDa, 6.25
Gene length, protein length	714 bp, 238 aa
Immediate neighbours	lutB, yvfU
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

FbpB regulon, FsrA regulon, 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

• BsubCyc: BSU34050

• 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:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU34050

• Structure:

• UniProt: O07020

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: lutA-lutB-lutC PubMed

• Expression browser: lutA 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:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 289 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 2918 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 799 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 738 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1342 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion: GP1612 amyE::p(lutA-lacZ cat), constructed with pGP2149 based on pAC5, available in Jörg Stülke's lab

• 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)