GlgP

• Description: glycogen phosphorylase
  
  

Gene name	glgP
Synonyms
Essential	no
Product	glycogen phosphorylase
Function	glycogen biosynthesis
MW, pI	91 kDa, 6.28
Gene length, protein length	2394 bp, 798 aa
Immediate neighbours	ytaB, glgA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

miscellaneous metabolic pathways, sporulation proteins, phosphoproteins

This gene is a member of the following regulons

SigE regulon

The gene

Basic information

• Locus tag: BSU30940

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: (1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate (according to Swiss-Prot)

• Protein family: glycogen phosphorylase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylation on (Thr-291 OR Ser-294) PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P39123

• KEGG entry: [3]

• E.C. number: 2.4.1.1

Expression and regulation

• Operon: glgB-glgC-glgD-glgA-glgP PubMed

• Sigma factor: SigE PubMed

• Regulation:
  • expressed early during sporulation in the mother cell (SigE) PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

J A Kiel, J M Boels, G Beldman, G Venema
Glycogen in Bacillus subtilis: molecular characterization of an operon encoding enzymes involved in glycogen biosynthesis and degradation.
Mol Microbiol: 1994, 11(1);203-18
[PubMed:8145641] [WorldCat.org] [DOI] (P p)