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* '''Description:''' phosphotyrosin protein phosphatase, antagonist to PtkA <br/><br/>
* '''Description:''' Enzyme I, general (non sugar-specific) component of the PTS. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein ([[PtsH |HPr]])  <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'''
|''ptpZ''
|''ptsI''
|-
|-
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''ywqE ''
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
|-
|-
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
|style="background:#ABCDEF;" align="center"| '''Essential''' || no
|-
|-
|style="background:#ABCDEF;" align="center"| '''Product''' || phosphotyrosin protein phosphatase, <br/>antagonist to PtkA
|style="background:#ABCDEF;" align="center"| '''Product''' || phosphotransferase system (PTS) enzyme I
|-
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || protein tyrosine dephosphorylation
|style="background:#ABCDEF;" align="center"|'''Function''' || PTS-dependent sugar transport
|-
|-
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 28 kDa, 6.66 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 62,9 kDa, 4.59
|-
|-
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 762 bp, 254 aa
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1710 bp, 570 amino acids
|-
|-
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ywqF]]'', ''[[ptkA]]''
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ptsH]]'', ''[[splA]]''
|-
|-
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB15641&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13264&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
|-
|-
|colspan="2" | '''Genetic context''' <br/> [[Image:ywqE_context.gif]]
|-
|-
|colspan="2" | '''Genetic context''' <br/> [[Image:ptsI_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/><br/>


=The gene=
=The gene=
Line 35: Line 37:
=== Basic information ===
=== Basic information ===


* '''Locus tag:''' BSU36240
* '''Locus tag:''' BSU13910


===Phenotypes of a mutant ===
===Phenotypes of a mutant ===
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=== Database entries ===
=== Database entries ===


* '''DBTBS entry:''' no entry
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ptsGHI.html]


* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG12509]
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10201]


=== Additional information===
=== Additional information===


=The protein=
=The protein=
Line 52: Line 53:
=== Basic information/ Evolution ===
=== Basic information/ Evolution ===


* '''Catalyzed reaction/ biological activity:''' Protein tyrosine phosphate + H<sub>2</sub>O = protein tyrosine + phosphate (according to Swiss-Prot)  
* '''Catalyzed reaction/ biological activity:''' Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine (according to Swiss-Prot) PEP-dependent autophosphorylation on His-189, transfer of the phosphoryl group to [[PtsH |HPr]] (His-15)


* '''Protein family:''' cpsB/capC family (according to Swiss-Prot)
* '''Protein family:''' PEP-utilizing enzyme family (according to Swiss-Prot) PEP-utilizing enzyme family


* '''Paralogous protein(s):'''
* '''Paralogous protein(s):'''
Line 63: Line 64:


* '''Domains:'''  
* '''Domains:'''  
**HPr binding site (N-Terminal Domain)
**pyruvate binding site (C-Terminal Domain)
**pyrophosphate/phosphate carrier histidine (central Domain)


* '''Modification:'''
* '''Modification:''' transient autophosphorylation on His-189, in vivo also phosphorylated on Ser-34 or Ser-36 [http://www.ncbi.nlm.nih.gov/pubmed/17218307 PubMed]


* '''Cofactor(s):'''
* '''Cofactor(s):''' Magnesium


* '''Effectors of protein activity:'''
* '''Effectors of protein activity:'''
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* '''Interactions:'''
* '''Interactions:'''


* '''Localization:'''
* '''Localization:''' cytoplasm (according to Swiss-Prot),  Cytoplasm


=== Database entries ===
=== Database entries ===
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* '''Structure:'''
* '''Structure:'''


* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P96717 P96717]
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P08838 P08838]


* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU36240]
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU13910]


* '''E.C. number:''' [http://www.expasy.org/enzyme/3.1.3.48 3.1.3.48]
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.3.9 2.7.3.9]  2.7.3.9]


=== Additional information===
=== Additional information===


=Expression and regulation=
=Expression and regulation=


* '''Operon:''' ''[[tkmA]]-[[ptkA]]-[[ptpZ]]-[[ywqF]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/12970183 PubMed]
* '''Operon:'''  
 
**''[[ptsG]]-[[ptsH]]-[[ptsI]]''
* '''[[Sigma factor]]:'''  
**''[[ptsH]]-[[ptsI]]''


* '''Regulation:'''  
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11902727 PubMed]
* '''Regulation:''' expression activated by glucose (4.3 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed],  induction by glucose (''[[ptsG]]''), constitutive (''[[ptsH]]'')


* '''Regulatory mechanism:'''  
* '''Regulatory mechanism:''' ''[[ptsG]]'': transcriptional antitermination via the [[GlcT]]-dependent RNA-switch


* '''Additional information:'''
* '''Additional information:'''
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=Biological materials =
=Biological materials =


* '''Mutant:'''
* '''Mutant:''' GP864 (ermC), available in [[Stülke]] lab


* '''Expression vector:'''
* '''Expression vector:''' pAG3 (His-tag), available in [[Galinier]] lab
       
* '''lacZ fusion:'''
* '''lacZ fusion:'''


* '''GFP fusion:'''
* '''GFP fusion:'''
* '''two-hybrid system:'''


* '''Antibody:'''
* '''Antibody:'''


=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]


=Your additional remarks=
=Your additional remarks=
Line 118: Line 126:
=References=
=References=


<pubmed>12970183, </pubmed>
<pubmed>12850135 17218307, </pubmed>
# Mijakovic I, Poncet S, Boël G, Mazé A, Gillet S, Decottignies P, Grangeasse C, Jamet E, Doublet P, Le Maréchal P, Deutscher J (2003) Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases. EMBO J 22:4709-4718. [http://www.ncbi.nlm.nih.gov/sites/entrez/12970183 PubMed]
# Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in ''Bacillus subtilis'': regulation of the central metabolic pathways. ''Metab Eng.'' '''5:''' 133-149 [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
# Frisby, D., and Zuber, P. 1994. Mutations in pts cause catabolite-resistant sporulation and altered regulation of spo0H in Bacillus subtilis. J. Bacteriol. 176: 2587-2595. [http://www.ncbi.nlm.nih.gov/sites/entrez/8169206  PubMed]
# Macek B, Mijakovic I, Olsen JV (2007) The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. ''Mol Cell Proteomics'' '''6(4):''' 697-707. [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed]

Revision as of 13:30, 8 June 2009

  • Description: Enzyme I, general (non sugar-specific) component of the PTS. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr)

Gene name ptsI
Synonyms
Essential no
Product phosphotransferase system (PTS) enzyme I
Function PTS-dependent sugar transport
MW, pI 62,9 kDa, 4.59
Gene length, protein length 1710 bp, 570 amino acids
Immediate neighbours ptsH, splA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
This image was kindly provided by SubtiList





The gene

Basic information

  • Locus tag: BSU13910

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine (according to Swiss-Prot) PEP-dependent autophosphorylation on His-189, transfer of the phosphoryl group to HPr (His-15)
  • Protein family: PEP-utilizing enzyme family (according to Swiss-Prot) PEP-utilizing enzyme family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • HPr binding site (N-Terminal Domain)
    • pyruvate binding site (C-Terminal Domain)
    • pyrophosphate/phosphate carrier histidine (central Domain)
  • Modification: transient autophosphorylation on His-189, in vivo also phosphorylated on Ser-34 or Ser-36 PubMed
  • Cofactor(s): Magnesium
  • Effectors of protein activity:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot), Cytoplasm

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism: ptsG: transcriptional antitermination via the GlcT-dependent RNA-switch
  • Additional information:

Biological materials

  • Mutant: GP864 (ermC), available in Stülke lab
  • Expression vector: pAG3 (His-tag), available in Galinier lab
  • lacZ fusion:
  • GFP fusion:
  • Antibody:

Labs working on this gene/protein

Josef Deutscher, Paris-Grignon, France

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

<pubmed>12850135 17218307, </pubmed>

  1. Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
  2. Frisby, D., and Zuber, P. 1994. Mutations in pts cause catabolite-resistant sporulation and altered regulation of spo0H in Bacillus subtilis. J. Bacteriol. 176: 2587-2595. PubMed
  3. Macek B, Mijakovic I, Olsen JV (2007) The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol Cell Proteomics 6(4): 697-707. PubMed
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