LutC

• Description: lactate catabolic enzyme
  
  

Gene name	lutC
Synonyms	yvbY
Essential	no
Product	unknown
Function	utilization of lactate
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	26 kDa, 5.157
Gene length, protein length	720 bp, 240 aa
Immediate neighbours	yvbX, lutB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

utilization of specific carbon sources, phosphoproteins

This gene is a member of the following regulons

FbpB regulon, FsrA regulon, LutR regulon, SinR regulon

The gene

Basic information

• Locus tag: BSU34030

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: UPF0707 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-97 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: O32259

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: lutA-lutB-lutC PubMed

• Expression browser: 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

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

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)