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PMID:20144229
| Citation |
Rangrez, AY, Abajy, MY, Keller, W, Shouche, Y and Grohmann, E (2010) Biochemical characterization of three putative ATPases from a new type IV secretion system of Aeromonas veronii plasmid pAC3249A. BMC Biochem. 11:10 |
|---|---|
| Abstract |
Type four secretion systems (TFSS) are bacterial macromolecular transport systems responsible for transfer of various substrates such as proteins, DNA or protein-DNA complexes. TFSSs encode two or three ATPases generating energy for the secretion process. These enzymes exhibit highest sequence conservation among type four secretion components. |
| Links |
PubMed PMC2831815 Online version:10.1186/1471-2091-11-10 |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Aeromonas/enzymology; Cobalt/chemistry; Hydrolysis; Magnesium/chemistry; Manganese/chemistry; Molecular Sequence Data; Plasmids; Protein Binding; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification; Secretory Pathway; Temperature |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0016887: ATPase activity |
ECO:0000314: |
F |
Fig. 6 - ATP hydrolysis assay measured ATP concentration via ATPase assay. |
complete | ||||
|
enables |
GO:0016887: ATPase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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