Difference between revisions of "BglP"
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|colspan="2" | '''Genetic context''' <br/> [[Image:bglP_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:bglP_context.gif]] | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
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+ | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=bglP_4033778_4035607_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:bglP_expression.png|500px]] | ||
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Revision as of 12:25, 23 April 2012
- Description: trigger enzyme: beta-glucoside-specific phosphotransferase system, EIIBCA of the PTS
Gene name | bglP |
Synonyms | sytA |
Essential | no |
Product | trigger enzyme: beta-glucoside-specific phosphotransferase system, EIIBCA |
Function | beta-glucoside uptake and phosphorylation, control of LicT activity |
Interactions involving this protein in SubtInteract: BglP | |
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism | |
MW, pI | 64 kDa, 6.809 |
Gene length, protein length | 1827 bp, 609 aa |
Immediate neighbours | bglH, yxxE |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
phosphotransferase systems, utilization of specific carbon sources, transcription factors and their control, trigger enzyme, membrane proteins, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU39270
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine (according to Swiss-Prot)
- 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:
- UniProt: P40739
- KEGG entry: [3]
- E.C. number: 2.7.1.69 9
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
- An antisense RNA is predicted for bglP PubMed
Biological materials
- Mutant: GP475 (erm), available in the Stülke lab
- Expression vector:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796]
[WorldCat.org]
[DOI]
(I p)
Juliane Ollinger, Kyung-Bok Song, Haike Antelmann, Michael Hecker, John D Helmann
Role of the Fur regulon in iron transport in Bacillus subtilis.
J Bacteriol: 2006, 188(10);3664-73
[PubMed:16672620]
[WorldCat.org]
[DOI]
(P p)
Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[PubMed:10627040]
[WorldCat.org]
[DOI]
(P p)
S Krüger, S Gertz, M Hecker
Transcriptional analysis of bglPH expression in Bacillus subtilis: evidence for two distinct pathways mediating carbon catabolite repression.
J Bacteriol: 1996, 178(9);2637-44
[PubMed:8626332]
[WorldCat.org]
[DOI]
(P p)
S Krüger, M Hecker
Regulation of the putative bglPH operon for aryl-beta-glucoside utilization in Bacillus subtilis.
J Bacteriol: 1995, 177(19);5590-7
[PubMed:7559347]
[WorldCat.org]
[DOI]
(P p)
D Le Coq, C Lindner, S Krüger, M Steinmetz, J Stülke
New beta-glucoside (bgl) genes in Bacillus subtilis: the bglP gene product has both transport and regulatory functions similar to those of BglF, its Escherichia coli homolog.
J Bacteriol: 1995, 177(6);1527-35
[PubMed:7883710]
[WorldCat.org]
[DOI]
(P p)