Difference between revisions of "Sandbox"

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* '''Description:''' HPr kinase/ phosphorylase<br/><br/>
+
* '''Description:''' write here <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
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|''hprK''
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|''lgt''
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''ptsK, yvoB ''
+
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''gerF, yvoC ''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''Product''' || HPr kinase/ phosphorylase
+
|style="background:#ABCDEF;" align="center"| '''Product''' || prolipoprotein diacylglyceryl transferase
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Function''' || carbon catabolite repression,
+
|style="background:#ABCDEF;" align="center"|'''Function''' || required for the lipid modification of prolipoproteins <br/>before their cleavage and translocation<br/> across the cytoplasmic membrane
−
phosphorylation of HPr and Crh proteins at Ser46
 
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 34 kDa, 4.906  
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 30 kDa, 8.96  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 930 bp, 310 aa  
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 807 bp, 269 aa  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[lgt]]'', ''[[nagA]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yvoD]]'', ''[[hprK]]''
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Hier soll was neues rein'''
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Hier soll was neues rein'''
 
|-
 
|-
−
|colspan="2" | '''Genetic context''' <br/> [[Image:hprK_context.gif]]
+
|colspan="2" | '''Genetic context''' <br/> [[Image:lgt_context.gif]]
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
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__TOC__
 
__TOC__
  
−
<br/><br/>
+
<br/><br/><br/><br/>
  
 
=The gene=
 
=The gene=
Line 39: Line 38:
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
−
 
−
no carbon catabolite repression
 
  
 
=== Database entries ===
 
=== Database entries ===
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* '''DBTBS entry:''' no entry
 
* '''DBTBS entry:''' no entry
  
−
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG14125]
+
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG12611]
  
 
=== Additional information===
 
=== Additional information===
Line 73: Line 70:
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
−
* '''Interactions:''' HprK-[[PtsH| HPr]], HprK-[[Crh]] [http://www.ncbi.nlm.nih.gov/sites/entrez/12009882 PubMed]
+
* '''Interactions:'''
  
−
* '''Localization:'''
+
* '''Localization:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Swiss prot entry:'''
 
* '''Swiss prot entry:'''
  
−
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU35000]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU34990]
  
 
* '''E.C. number:'''
 
* '''E.C. number:'''
Line 93: Line 90:
 
* '''Operon:'''  
 
* '''Operon:'''  
  
−
* '''Sigma factor:'''  
+
* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
−
 
−
[[Josef Deutscher]], Paris-Grignon, France
 
−
 
−
[[Stülke|Jörg Stülke]], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
 
−
 
−
[[Wolfgang Hillen]], Erlangen University, Germany [http://www.biologie.uni-erlangen.de/mibi/index2.html Homepage]
 
−
 
−
[[Anne Galinier]], University of Marseille, France
 
  
 
=Your additional remarks=
 
=Your additional remarks=
Line 129: Line 118:
 
=References=
 
=References=
  
−
'''review'''
+
# Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing ''Bacillus subtilis'' by divergent approaches. Proteomics '''8:''' 4123-4136 [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
−
# Nessler S, Fieulaine S, Poncet S, Galinier A, Deutscher J, Janin J (2003) HPr kinase/phosphorylase, the sensor enzyme of catabolite repression in Gram-positive bacteria: structural aspects of the enzyme and the complex with its protein substrate. J Bacteriol 185:4003-4010. [http://www.ncbi.nlm.nih.gov/sites/entrez/12837773 PubMed]
 
−
 
 
−
'''general/ physiology'''
 
−
# Reizer, J., Hoischen, C., Titgemeyer, F., Rivolta, C., Rabus, R., Stülke, J., Karamata, D., Saier, M. H., Jr., & Hillen, W. (1998) A novel bacterial protein kinase that controls carbon catabolite repression. Mol. Microbiol. 27: 1157-1169. [http://www.ncbi.nlm.nih.gov/sites/entrez/9570401 PubMed]
 
−
# Galinier A, Kravanja M, Engelmann R, Hengstenberg W, Kilhoffer MC, Deutscher J, Haiech J (1998) New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression. Proc Natl Acad Sci USA 95:1823-1828. [http://www.ncbi.nlm.nih.gov/sites/entrez/9465101 PubMed]
 
−
# Ludwig, H., Rebhan, N., Blencke, H.-M., Merzbacher, M. & Stülke, J. (2002) Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation. Mol. Microbiol. 45: 543-553. [http://www.ncbi.nlm.nih.gov/sites/entrez/12123463 PubMed]
 
−
# Singh, K. D., Schmalisch, M. H., Stülke, J. & Görke, B. (2008) Carbon catabolite repression in Bacillus subtilis: A quantitative analysis of repression exerted by different carbon sources. J. Bacteriol. 190: 7275-7284. [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537 PubMed]
 
−
 
 
−
'''enzymatic properties, mutation analysis'''
 
−
# Mijakovic I, Poncet S, Galiner A, Monedero V, Fieulaine S, Janin J, Nessler S, Marquez JA, Scheffzek K, Hasenbein S, Hengstenberg W, Deutscher J: Pyrophosphate-producing protein dephosphorylation by HPr kinase/ phosphorylase: a relic of early life? Proc Natl Acad Sci USA 2002, 99:13442-13447.  [http://www.ncbi.nlm.nih.gov/sites/entrez/12359880 PubMed]
 
−
# Monedero V, Poncet S, Mijakovic I, Fieulaine S, Dossonet V, Martin-Verstraete I, Nessler S, Deutscher J (2001) Mutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolism. EMBO J 20:3928-3937. [http://www.ncbi.nlm.nih.gov/sites/entrez/11483496 PubMed]
 
−
# Hanson K. G., Steinhauer, K., Reizer, J., Hillen, W. & Stülke, J. (2002) HPr kinase/phosphatase of Bacillus subtilis: Expression of the gene and effects of mutations on enzyme activity, growth, and carbon catabolite repression. Microbiology 148: 1805-1811. [http://www.ncbi.nlm.nih.gov/sites/entrez/12055300 PubMed]
 
−
# Jault J M, Fieulaine S, Nessler S, Gonzalo P, Di Pietro A, Deutscher J, Galinier A (2000) The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding. J Biol Chem 275:1773-1780. [http://www.ncbi.nlm.nih.gov/sites/entrez/10636874 PubMed]
 
−
# Ramström H, Sanglier S, Leize-Wagner E, Philippe C, van Dorsselaer A, Haiech J (2003) Properties and regulation of the bifunctional enzyme HPr kinase/phosphatase in Bacillus subtilis. J Biol Chem 278:1174-1185. [http://www.ncbi.nlm.nih.gov/sites/entrez/12411438 PubMed]
 
−
# Galinier, A., Lavergne, J.-P., Geourjon, C., Fieulaine, S., Nessler, S. & Jault, J.-M. (2002) A new family of phosphotransferases with a P-loop motif. J. Biol. Chem. 277, 11362-11367. [http://www.ncbi.nlm.nih.gov/sites/entrez/11796714 PubMed]
 
−
# Lavergne, J.-P., Jault, J.-M. & Galinier, A. (2002) Insights into the functioning of ''Bacillus subtilis'' HPr kinase/phosphatase: affinity for its protein substrates and role of cations and phosphate. Biochemistry 41, 6218-6225. [http://www.ncbi.nlm.nih.gov/sites/entrez/12009882 PubMed]
 
−
# Pompeo, F., Granet, Y., Lavergne, J.-P., Grangeasse, C., Nessler, S., Jault, J.-M. & Galinier, A. (2003) Regulation and mutational analysis of the HPr kinase/phosphorylase from ''Bacillus subtilis''. Biochemistry 42, 6762-6771. [http://www.ncbi.nlm.nih.gov/sites/entrez/12779331 PubMed]
 
−
 
 
−
'''structure analysis'''
 
−
# Márquez, J. A., Hasenbein, S., Koch, B., Fieulaine, S., Nessler, S., Russell, R. B., Hengstenberg, W. & Scheffzek, K. (2002) Structure of the full-length HPr kinase/phosphatase from ''Staphylococcus xylosus'' at 1.95 Å resolution: mimicking the product/substrate of the phosphotransfer reactions. Proc. Natl. Acad. Sci. USA 99, 3458-3463. [http://www.ncbi.nlm.nih.gov/sites/entrez/11904409 PubMed]
 
−
# Allen, G.S., Steinhauer, K., Hillen, W., Stülke, J. & Brennan, R.G. (2003) Crystal structure of HPr kinase/phosphatase from ''Mycoplasma pneumoniae''. J. Mol. Biol. 326, 1203-1217. [http://www.ncbi.nlm.nih.gov/sites/entrez/12589763 PubMed]
 
−
# Fieulaine, S., Morera, S., Poncet, S., Mijakovic, I., Galinier, A., Janin, J., Deutscher, J., and Nessler, S. (2002) X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr. Proc Natl Acad Sci U S A 99: 13437-13441. [http://www.ncbi.nlm.nih.gov/sites/entrez/12359875 PubMed]
 
−
 
 
−
'''HprK as target for antimicrobial compounds'''
 
−
# Ramström, H. et al. (2004) Heterocylic bis-cations as starting hits for design of inhibitors of the bifunctional enzyme histidine-containing protein kinase/ phosphatase from ''Bacillus subtilis''. J. Med. Chem. 47, 2264-2275. [http://www.ncbi.nlm.nih.gov/sites/entrez/15084125 PubMed]
 
−
 
 
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 17:36, 15 April 2009

  • Description: write here

Gene name lgt
Synonyms gerF, yvoC
Essential no
Product prolipoprotein diacylglyceryl transferase
Function required for the lipid modification of prolipoproteins
before their cleavage and translocation
across the cytoplasmic membrane
MW, pI 30 kDa, 8.96
Gene length, protein length 807 bp, 269 aa
Immediate neighbours yvoD, hprK
Hier soll was neues rein
Genetic context
Lgt context.gif
This image was kindly provided by SubtiList





The gene

Basic information

  • Coordinates:

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:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: membrane associated PubMed

Database entries

  • Structure:
  • 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

  1. Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
  2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
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