Difference between revisions of "PtsI"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.proteopedia.org/wiki/index.php/2hwg 2HWG] (Enzyme I from ''E. coli'') |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P08838 P08838] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P08838 P08838] |
Revision as of 11:16, 5 August 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 |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
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
|
Contents
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: 2HWG (Enzyme I from E. coli)
- UniProt: P08838
- KEGG entry: [3]
- E.C. number: 2.7.3.9 2.7.3.9]
Additional information
Expression and regulation
- Sigma factor: SigA PubMed
- Regulation: expression activated by glucose (4.3 fold) PubMed, induction by glucose (ptsG), constitutive (ptsH)
- 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