LutB

• Description: lactate catabolic enzyme
  
  

Gene name	lutB
Synonyms	yvfW
Essential	no
Product	lactate oxidase
Function	lactate utilization
Gene expression levels in SubtiExpress: lutB
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	53 kDa, 5.848
Gene length, protein length	1437 bp, 479 aa
Immediate neighbours	lutC, lutA
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, phosphoproteins

This gene is a member of the following regulons

FbpB regulon, FsrA regulon, LutR regulon, SinR regulon

The gene

Basic information

• Locus tag: BSU34040

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:
  • phosphorylated on Arg-33 PubMed

• Cofactor(s): contains an iron-sulfur cluster

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: O07021

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: lutA-lutB-lutC PubMed

• Expression browser: lutB PubMed

• Sigma factor:

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

• Regulatory mechanism:
  • SinR: transcription repression PubMed
  • dual repression by LutR (inducer lactate) and SinR 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)

Gregory T Smaldone, Olga Revelles, Ahmed Gaballa, Uwe Sauer, Haike Antelmann, John D Helmann
A global investigation of the Bacillus subtilis iron-sparing response identifies major changes in metabolism.
J Bacteriol: 2012, 194(10);2594-605
[PubMed:22389480] [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)

Ahmed Gaballa, Haike Antelmann, Claudio Aguilar, Sukhjit K Khakh, Kyung-Bok Song, Gregory T Smaldone, John D Helmann
The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins.
Proc Natl Acad Sci U S A: 2008, 105(33);11927-32
[PubMed:18697947] [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)