Difference between revisions of "BglP"

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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=BglP BglP]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=BglP BglP]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbohydrate_metabolic_pathways.html Sugar catabolism]'''
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=bglP bglP]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 64 kDa, 6.809   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 64 kDa, 6.809   

Revision as of 12:00, 7 January 2014

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
Gene expression levels in SubtiExpress: bglP
Interactions involving this protein in SubtInteract: BglP
Metabolic function and regulation of this protein in SubtiPathways:
bglP
MW, pI 64 kDa, 6.809
Gene length, protein length 1827 bp, 609 aa
Immediate neighbours bglH, yxxE
Sequences Protein DNA DNA_with_flanks
Genetic context
BglP context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
BglP expression.png















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

CcpA regulon, LicT regulon

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)
  • Protein family: PTS permease, sucrose permease (Scr) family PubMed
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism:
    • CcpA: transcription repression, (CcpA binding site overlaps -35 region) PubMed
    • LicT-dependent RNA switch (antitermination, lack of LicT-dependent antitermination in the presence of gucose due to the requirement of LicT to be phosphorylated by HPr PubMed

Biological materials

  • Mutant: GP475 (erm), available in the Stülke lab
  • Expression vector:
    • pGP1290 (C-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP382), available in Stülke lab,
    • pGP1300 (expression of bglP in B. subtilis, in pBQ200), available in Stülke lab
  • lacZ fusion: pGP600 (in pAC6), available in Stülke lab
  • GFP fusion:
  • CFP fusion: B. subtilis GP1266 bglP-cfp ermC- without terminator, available in Jörg Stülke's lab
  • YFP fusion: B. subtilis GP1274 bglP-yfp ermC- without terminator, available in Jörg Stülke's lab
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Fabian M Rothe, Christoph Wrede, Martin Lehnik-Habrink, Boris Görke, Jörg Stülke
Dynamic localization of a transcription factor in Bacillus subtilis: the LicT antiterminator relocalizes in response to inducer availability.
J Bacteriol: 2013, 195(10);2146-54
[PubMed:23475962] [WorldCat.org] [DOI] (I p)

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

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)