Difference between revisions of "PtsG"

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<pubmed> 18086213 </pubmed>
 
<pubmed> 18086213 </pubmed>
 
==Original publications==
 
==Original publications==
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<pubmed>10627040 ,12850135 ,18763711 ,11902727 ,9765562 ,9513271 ,1956301 ,10543968 ,17074746 ,15155854 ,14527945 ,1508157 ,2120236 9593197 8418852 1581296 1316146 1733770 1942043 1911744 1906345 20081037 22846916 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:03, 1 August 2012

  • Description: trigger enzyme: major glucose permease of the PTS, EIICBA(Glc) and control of GlcT activity

Gene name ptsG
Synonyms ptsX, crr
Essential no
Product trigger enzyme: glucose-specific enzyme IICBA component of the PTS
Function glucose transport and phosphorylation, control of GlcT activity
Interactions involving this protein in SubtInteract: PtsG
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism, Sugar catabolism
MW, pI 75,3 kDa, 5.40
Gene length, protein length 2097 bp, 699 amino acids
Immediate neighbours glcT, ptsH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PtsG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PtsG expression.png




























Categories containing this gene/protein

phosphotransferase systems, carbon core metabolism, transcription factors and their control, trigger enzyme, membrane proteins, phosphoproteins

This gene is a member of the following regulons

GlcT regulon, stringent response

The gene

Basic information

  • Locus tag: BSU13890

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: transport and phosphorylation of glucose, receives a phosphate from HPr at the IIA domain (His-620), the phosphate group is then transferred to the IIB domain (Cys-461) an finally to the incoming glucose. In the absence of glucose, PtsG phosphorylates and thereby inactivates the transcriptional antiterminator GlcT.
  • Protein family: PTS permease, glucose permease (Glc) family PubMed, PTS enzyme II
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • 11x transmembrane domain (16–36, 89–109, 139–159, 180–200, 233–253, 283–303, 313–333, 338–358, 365–385, 388–408)
    • PTS EIIC domain ( 1-424)
    • PTS EIIB domain (439–520)
    • PTS EIIA domain (568–672)
  • Modification: transient phosphorylation (HPr-dependent) on His-620, then internal phosphotransfer from His-620 to Cys-461
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1AX3 (IIA domain), 1GPR (IIA domain), IIA domain NCBI, NMR IIA domain NCBI
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expression activated by glucose (32 fold) (GlcT) PubMed
    • subject to negative stringent control upon lysine starvation PubMed
  • Regulatory mechanism:
    • transcriptional antitermination via the GlcT-dependent RNA switch PubMed
    • stringent response: due to presence of guanine at +1 position of the transcript PubMed
  • Additional information:

Biological materials

  • Mutants: all available in Stülke lab
    • QB5435 (cat)
    • QB5436 (spc)
    • QB5445 (erm)
    • GP778 (replacement of glcT and the ptsG-ptsH-ptsI operon by a spc cassette)
    • GP926 (substitution of glcT and ptsG by a tet cassette)
  • Expression vector:
  • GFP fusion:
  • Antibody:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

Reviews

Fabian M Commichau, Jörg Stülke
Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression.
Mol Microbiol: 2008, 67(4);692-702
[PubMed:18086213] [WorldCat.org] [DOI] (P p)

Original publications