Difference between revisions of "LutA"

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(Biological materials)
(Biological materials)
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* '''Expression vector:'''
* '''Expression vector:'''
* '''lacZ fusion:''' amyE::P(lutA-lacZ cat), constructed with [[pAC5]]
* '''lacZ fusion:''' amyE::p(lutA-lacZ cat), constructed with [[pAC5]]
* '''GFP fusion:'''
* '''GFP fusion:'''

Revision as of 09:50, 28 January 2014

  • 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:
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
YvfV context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LutA expression.png

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

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

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:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion: amyE::p(lutA-lacZ cat), constructed with pAC5
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Richard Losick, Harvard Univ., Cambridge, USA homepage

Your additional remarks


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)