Difference between revisions of "ManP"

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|style="background:#ABCDEF;" align="center"|'''Function''' || mannose uptake and phosphorylation, control of ManR activity
 
|style="background:#ABCDEF;" align="center"|'''Function''' || mannose uptake and phosphorylation, control of ManR activity
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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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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 61 kDa, 6.715   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 61 kDa, 6.715   

Revision as of 12:00, 11 June 2009

  • Description: trigger enzyme: mannose-specific phosphotransferase system, EIIBCA

Gene name manP
Synonyms yjdD
Essential no
Product trigger enzyme: mannose-specific phosphotransferase system, EIIBCA
Function mannose uptake and phosphorylation, control of ManR activity
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 61 kDa, 6.715
Gene length, protein length 1767 bp, 589 aa
Immediate neighbours manR, manA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ManP context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU12010

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: PTS permease, fructose/ mannitol permease (Fru) family PubMed
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on Ser-365 PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:

Database entries

  • Swiss prot entry:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

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)

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)

  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
  2. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed
  3. Reizer, J., Bachem, S., Reizer, A., Arnaud, M., Saier Jr., M. H. & Stülke, J. (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
  4. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed