Difference between revisions of "PtsH"

From SubtiWiki
Jump to: navigation, search
(Biological materials)
(Biological materials)
Line 124: Line 124:
 
=Biological materials =
 
=Biological materials =
  
* '''Mutant:''' MZ303 (cat), GP507 ptsH1 (S46A), GP506 (ptsH-H15A), GGP778 (replacement of ''glcT'' and the ''ptsGHI'' operon by a spc cassette), available in [[Stülke]] lab
+
* '''Mutant:''' MZ303 (cat), GP507 ptsH1 (S46A), GP506 (ptsH-H15A), GP778 (replacement of ''glcT'' and the ''ptsGHI'' operon by a spc cassette), available in [[Stülke]] lab
  
 
* '''Expression vector:'''  
 
* '''Expression vector:'''  

Revision as of 12:40, 13 September 2010

  • Description: HPr, General component of the sugar phosphotransferase system (PTS).

Gene name ptsH
Synonyms
Essential no
Product histidine-containing phosphocarrier
protein HPr of the PTS
Function PTS-dependent sugar transport
and carbon catabolite repression
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism, Sugar catabolism
MW, pI 9,1 kDa, 4.58
Gene length, protein length 264 bp, 88 amino acids
Immediate neighbours ptsG, ptsI
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PtsH context.gif
This image was kindly provided by SubtiList








The gene

Basic information

  • Locus tag: BSU13900

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-histidine (according to Swiss-Prot) Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-histidine
  • Protein family: HPr domain (according to Swiss-Prot) HPr family
  • Paralogous protein(s): Crh

Extended information on the protein

  • Kinetic information:
  • Domains: HPr Domain (2–88)
  • Modification:
    • transient phosphorylation by Enzyme I of the PTS on His-15
    • regulatory phosphorylation on Ser-46 by HprK PubMed
    • an extensive study on in vivo HPr phosphorylation can be found in Singh et al. (2008) PubMed
    • weak phosphorylation on Ser-12 PubMed
    • in vitro phosphorylated by PrkC on Ser-12 PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasm (according to Swiss-Prot), Cytoplasm PubMed

Database entries

  • Structure: 1KKM (complex of L. casei HprK with B. subtilis HPr-Ser-P), 1KKL (complex of Lactobacillus casei HprK with B. subtilis HPr), 2HID (NMR)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expression activated by glucose (2 fold) (GlcT) PubMed
    • the ptsH promoter is constitutive PubMed
    • subject to negative stringent control upon amino acid limitation (due to control of ptsG transcription initiation) PubMed
  • Additional information:

Biological materials

  • Mutant: MZ303 (cat), GP507 ptsH1 (S46A), GP506 (ptsH-H15A), GP778 (replacement of glcT and the ptsGHI operon by a spc cassette), available in Stülke lab
  • Expression vector:
    • pGP438 (with N-terminal Strep-tag, in pGP172), available in Stülke lab
    • pAG2 (His-tag), available in Anne Galinier lab
    • pGP371(expression / purification of HPr-S46A, with His-tag from E. coli, in pWH844), available in Stülke lab
    • pGP1415 (HPr, expression in B. subtilis, from pBQ200), available in Stülke lab
    • pGP961 (HPr, expression in B. subtilis with N-terminal Strep-tag, for SPINE, available in Stülke lab
    • pGP1416 (HPr-H15A, expression in B. subtilis, from pBQ200), available in Stülke lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Görke lab
  • Antibody: available in Stülke lab

Labs working on this gene/protein

Josef Deutscher, Paris-Grignon, France

Jörg Stülke, University of Göttingen, Germany Homepage

Wolfgang Hillen, Erlangen University, Germany Homepage

Richard Brennan, Houston, Texas, USA Homepage

Boris Görke, University of Göttingen, Germany Homepage

Anne Galinier, University of Marseille, France

Your additional remarks

References