Difference between revisions of "LutC"

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(Categories containing this gene/protein)
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* '''Modification:'''
 
* '''Modification:'''
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** phosphorylated on Arg-97 {{PubMed|22517742}}
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
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=References=
 
=References=
  
<pubmed>22427629,19201793, 19201793 </pubmed>
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<pubmed>22427629,19201793, 19201793 22517742</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:51, 21 April 2012

  • 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
YvbY context.gif
This image was kindly provided by SubtiList







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]

Additional information

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:

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:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Richard Losick, Harvard Univ., Cambridge, USA homepage

Your additional remarks

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)