Difference between revisions of "GamP"

From SubtiWiki
Jump to: navigation, search
Line 13: Line 13:
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Function''' || glucosamine uptake and phosphorylation
 
|style="background:#ABCDEF;" align="center"|'''Function''' || glucosamine uptake and phosphorylation
 +
|-
 +
|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]'''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 67 kDa, 5.472   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 67 kDa, 5.472   

Revision as of 11:45, 11 June 2009

  • Description: glucosamine-specific phosphotransferase system, EIICBA

Gene name gamP
Synonyms ybfS, yzfA
Essential no
Product glucosamine-specific phosphotransferase system, EIICBA
Function glucosamine uptake and phosphorylation
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 67 kDa, 5.472
Gene length, protein length 1893 bp, 631 aa
Immediate neighbours gltP, gamA
Gene sequence (+200bp) Protein sequence
Genetic context
GamP context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU02350

Phenotypes of a mutant

delayed growth with glucosamine as the single carbon source PubMed

Database entries

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

Additional information

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, 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

  • 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)

  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. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed