Difference between revisions of "PtsI"
|  (→Expression and regulation) |  (→Database entries) | ||
| Line 44: | Line 44: | ||
| * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ptsGHI.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ptsGHI.html] | ||
| − | * '''SubtiList entry:'''  | + | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10201] | 
| === Additional information=== | === Additional information=== | ||
Revision as of 11:38, 12 January 2009
-  Description: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar 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 | transfers phosphate from PEP to HPr | 
| 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 File:GenE context.gif | |
Contents
The gene
Basic information
- Coordinates:
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
- 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:
- 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

