Difference between revisions of "PtsI"
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' PEP-dependent autophosphorylation on His-189, transfer of the phosphoryl group to [[PtsH |HPr]] (His-15) |
* '''Protein family:''' PEP-utilizing enzyme family | * '''Protein family:''' PEP-utilizing enzyme family |
Revision as of 18:04, 13 January 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 | pstH, splA |
Gene sequence (+200bp) | Protein sequence |
Genetic context |
Contents
The gene
Basic information
- Coordinates: 1458959 - 1460668
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: PEP-dependent autophosphorylation on His-189, transfer of the phosphoryl group to HPr (His-15)
- Protein family: 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: phosphorylation (Ser-44 or Ser-46)
- Cofactor(s): Magnesium
- Effectors of protein activity:
- Interactions:
- Localization: Cytoplasm
Database entries
- Structure:
- Swiss prot entry: [3]
- KEGG entry: [4]
- E.C. number: [5]
Additional information
Expression and regulation
- Additional information:
Biological materials
Labs working on this gene/protein
Josef Deutscher, Paris-Grignon, France
Jörg Stülke, University of Göttingen, Germany Homepage