BglP

• Description: trigger enzyme: beta-glucoside-specific phosphotransferase system, EIIBC
  
  

Gene name	bglP
Synonyms	sytA
Essential	no
Product	trigger enzyme: beta-glucoside-specific phosphotransferase system, EIIBC
Function	beta-glucoside uptake and phosphorylation, control of LicT activity
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

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:

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• Structure:

• Swiss prot entry: P40739

• KEGG entry: [3]

• E.C. number: 2.7.1.69 9

Expression and regulation

• Operon: bglP-bglH-yxiE PubMed

• Sigma factor: SigA

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

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

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

1. 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

1. Le Coq, D., Lindner, C., Krüger, S., Steinmetz, M. & Stülke, J. (1995) New ß-glucosides (bgl) genes in Bacillus subtilis: The bglP gene product has both transport and regulatory functions, similar to that of the Escherichia coli BglF protein. J. Bacteriol. 177: 1527-1535. PubMed
2. Krüger, S., Gertz, S. & Hecker, M. Transcriptional analysis of bglPH expression in Bacillus subtilis: Evidence for two distinct pathways mediating carbon catabolite repression. J. Bacteriol. 178, 2637-2644 (1996). PubMed
3. Krüger, S. and Hecker, M. (1995) Regulation of the putative bglPH operon for aryl-ß-glycoside utilization in Bacillus subtilis. J. Bacteriol. 177, 5590-5597. PubMed
4. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed