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BORBU:O51190
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| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status | |
|---|---|---|---|---|---|---|---|---|---|---|---|
|
protected |
enables |
GO:0008270 |
zinc ion binding |
GO_REF:0000002 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR000962 |
F |
Seeded From UniProt |
||
|
protected |
enables |
GO:0008270 |
zinc ion binding |
GO_REF:0000002 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR000962 |
F |
Seeded From UniProt |
||
|
public |
GO:0015972 |
guanosine pentaphosphate metabolic process |
PMID:30478087 |
ECO:0007110 |
thin layer chromatography evidence used in manual assertion |
P |
The authors generated a mutant strain of Borrelia burgdorferi with the dksA gene knocked out. Using thin-layer chromatography, they measured the levels of (p)ppGpp produced by both wild-type and ΔdksA mutants under starvation conditions (figure 7A). When these results were quantified and normalized to levels of (p)ppGpp+GTP, the authors found that the ΔdksA mutant produced significantly higher levels of (p)ppGpp than wild-type (figure 7B). Reinsertion of the dksA gene through a plasmid vector containing the dksA ORF (pDksA) restored production levels of (p)ppGpp comparable to that of the wild-type strain. This indicates that the dksA gene plays a role in regulation of guanosine pentaphosphate metabolism. |
complete |
| Cancel |
