Difference between revisions of "PhoD"
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* '''[[Cofactors]]:''' | * '''[[Cofactors]]:''' | ||
− | ** one Fe and two Ca {{PubMed|25217636}} | + | ** one Fe<sup>3+</sup> and two Ca<sup>2+</sup> {{PubMed|25217636}} |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' |
Revision as of 08:21, 19 September 2014
- Description: phosphodiesterase/alkaline phosphatase
Gene name | phoD |
Synonyms | ycbS |
Essential | no |
Product | phosphodiesterase/alkaline phosphatase |
Function | aquisition of phosphate upon phosphoate starvation |
Gene expression levels in SubtiExpress: phoD | |
Interactions involving this protein in SubtInteract: PhoD | |
Metabolic function and regulation of this protein in SubtiPathways: PhoD | |
MW, pI | 62 kDa, 8.394 |
Gene length, protein length | 1668 bp, 556 aa |
Immediate neighbours | yczK, tatAD |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU02620
Phenotypes of a mutant
Database entries
- BsubCyc: BSU02620
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: A phosphate monoester + H2O = an alcohol + phosphate (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization: extracellular (signal peptide) PubMed, secreted by the TatAD-TatCD complex PubMed
Database entries
- BsubCyc: BSU02620
- UniProt: P42251
- KEGG entry: [3]
- E.C. number: 3.1.3.1
Additional information
Expression and regulation
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Oscar Kuipers, University of Groningen, The Netherlands Homepage
Your additional remarks
References
Reviews
Original publications