Difference between revisions of "LutA"
(→Biological materials) |
|||
Line 37: | Line 37: | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
− | + | <br/><br/> | |
− | |||
− | |||
− | |||
− | |||
= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
Line 69: | Line 65: | ||
=== Additional information=== | === Additional information=== | ||
− | |||
− | |||
− | |||
=The protein= | =The protein= | ||
Line 87: | Line 80: | ||
* '''Kinetic information:''' | * '''Kinetic information:''' | ||
− | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
− | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
Line 117: | Line 110: | ||
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yvfV_3494985_3495701_-1 lutA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yvfV_3494985_3495701_-1 lutA] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' induction by lactate [http://www.ncbi.nlm.nih.gov/sites/entrez/19201793 PubMed] | * '''Regulation:''' induction by lactate [http://www.ncbi.nlm.nih.gov/sites/entrez/19201793 PubMed] | ||
Line 136: | Line 129: | ||
* '''Expression vector:''' | * '''Expression vector:''' | ||
− | * '''lacZ fusion:''' amyE::p(lutA-lacZ cat), constructed with [[pAC5]] | + | * '''lacZ fusion:''' amyE::p(lutA-lacZ cat), constructed with [[pAC5]], available in [[ Jörg Stülke]]'s lab |
* '''GFP fusion:''' | * '''GFP fusion:''' | ||
Line 152: | Line 145: | ||
=References= | =References= | ||
− | <pubmed>22427629,16430695 | + | <pubmed>22427629,16430695,19201793 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:20, 31 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: lutA | |
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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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:
- Modification:
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: O07020
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation: induction by lactate PubMed
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion: amyE::p(lutA-lacZ cat), constructed with pAC5, available in Jörg Stülke's lab
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Richard Losick, Harvard Univ., Cambridge, USA homepage
Your additional remarks
References
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)