Difference between revisions of "LutC"
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[[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 This image was kindly provided by SubtiList
|
Contents
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:
- UniProt: O32259
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation: induction by lactate 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
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)