Difference between revisions of "LutB"
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=The protein= | =The protein= | ||
Revision as of 17:44, 30 November 2010
- Description: lactate catabolic enzyme
Gene name | lutB |
Synonyms | yvfW |
Essential | no |
Product | lactate oxidase |
Function | lactate utilization |
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 |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
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]
Additional information
Categories containing this gene/protein
utilization of specific carbon sources
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:
- Cofactor(s): contains an iron-sulfur cluster
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: O07021
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- 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
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)