BglP

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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:
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
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:
  • 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,
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

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)