Difference between revisions of "LevE"
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=== Basic information === | === Basic information === | ||
− | * '''Locus tag:''' | + | * '''Locus tag:''' BSU27060 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P26380 P26380] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P26380 P26380] | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU27060] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.1.69 2.7.1.69] | * '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.1.69 2.7.1.69] |
Revision as of 11:44, 3 June 2009
- Description: trigger enzyme: fructose-specific phosphotransferase system, EIIB component
Gene name | levE |
Synonyms | sacL |
Essential | no |
Product | trigger enzyme: fructose-specific phosphotransferase system, EIIB component
fructose-specific enzyme IIB (EC 2.7.1.69) |
Function | fructose uptake and phosphorylation, control of LevR activity |
MW, pI | 17 kDa, 9.444 |
Gene length, protein length | 486 bp, 162 aa |
Immediate neighbours | levF, levD |
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: BSU27060
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate (according to Swiss-Prot)
- Protein family: PTS permease, mannose permease (Man) family PubMed
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure: 1BLE
- Swiss prot entry: P26380
- KEGG entry: [2]
- E.C. number: 2.7.1.69
Additional information
Expression and regulation
- Regulation: repressed by glucose (CcpA) , carbon catabolite repression, induction by fructose
- Regulatory mechanism: CcpA: transcription repression, catabolite repression: transcription repression by CcpA, transcription activator LevR is less active in the presence of glucose; induction: transcription activation by LevR
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
- Reizer et al. (1999) Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis. Microbiology 145: 3419-3429 PubMed
- Martin-Verstraete, I., Débarbouillé, M., Klier, A., and Rapoport, G. (1990) Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon. J Mol Biol 214: 657-671. PubMed
- Martin-Verstraete, I., Charrier, V., Stülke, J., Galinier, A., Erni, B., Rapoport, G., & Deutscher, J. (1998) Antagonistic effects of dual PTS catalyzed phosphorylation on the Bacillus subtilis transcriptional activator LevR. Mol. Microbiol. 28: 293-303. PubMed
- Schauder S, Nunn RS, Lanz R, Erni B, Schirmer T. 1998. Crystal structure of the IIB subunit of a fructose permease (IIBLev) from Bacillus subtilis. J. Mol. Biol. 276:591-602. PubMed
- Seip, S., R. Lanz, R. Gutknecht, K. Flükiger, and B. Erni. 1997. The fructose transporter of Bacillus subtilis encoded by the lev operon. Backbone assignment and secondary structure of the IIBLev subunit. Eur. J. Biochem. 243: 306-314. PubMed
- Charrier V, Deutscher J, Martin-Verstraete I (1997b) Protein phosphorylation chain of a Bacillus subtilis fructose-specific phosphotransferase system and its participation in regulation of the expression of the lev operon. Biochemistry 36:1163-1172. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed