Difference between revisions of "NagP"

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|style="background:#ABCDEF;" align="center"|'''Function''' || N-acetylglucosamine uptake and phosphorylation
 
|style="background:#ABCDEF;" align="center"|'''Function''' || N-acetylglucosamine uptake and phosphorylation
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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''' || 48 kDa, 7.127   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 48 kDa, 7.127   

Revision as of 12:02, 11 June 2009

  • Description: N-acetylglucosamine-specific phosphotransferase system, EIICB

Gene name nagP
Synonyms yflF
Essential no
Product N-acetylglucosamine-specific phosphotransferase system, EIICB
Function N-acetylglucosamine uptake and phosphorylation
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 48 kDa, 7.127
Gene length, protein length 1356 bp, 452 aa
Immediate neighbours yflG, ltaS
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
NagP context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU07700

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 EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate (according to Swiss-Prot)
  • Protein family: PTS permease, glucose permease (Glc) 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), membrane associated PubMed

Database entries

  • Structure:
  • KEGG entry: [2]

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

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I 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)

H L Mobley, R J Doyle, U N Streips, S O Langemeier
Transport and incorporation of N-acetyl-D-glucosamine in Bacillus subtilis.
J Bacteriol: 1982, 150(1);8-15
[PubMed:6174502] [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. Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 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. Mobley HL, Doyle RJ, Streips UN, Langemeier SO. (1982) Transport and incorporation of N-acetyl-D-glucosamine in Bacillus subtilis. J Bacteriol. Apr;150(1): 8-15. PubMed
  5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed