BglP

• 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
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:
  • BglP-HPr, BglP-LicT

• Localization: cell membrane PubMed

Database entries

• Structure:

• UniProt: P40739

• KEGG entry: [3]

• E.C. number: 2.7.1.69 9

Expression and regulation

• Operon: bglP-bglH-yxiE PubMed

• Expression browser: bglP PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (CcpA, LicT) PubMed
  • induced by salicin (LicT) PubMed

• 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

• Additional information:
  • An antisense RNA is predicted for bglP 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:

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, Epub ahead of print. 
PubMed:23475962

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)

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)