FetP (YggX-family probable Fe(2+)-trafficking protein, Vapar_2982) in Variovorax paradoxus S110 is a 90-amino-acid predicted cytosolic iron-binding protein (HAMAP rule MF_00686, InterPro IPR007457). Based on conserved YggX family membership, it is predicted to act as a mediator in intracellular iron transactions between iron acquisition pathways and iron-requiring processes such as the synthesis and repair of iron-sulfur clusters in biosynthetic enzymes.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005506 iron ion binding | IEA GO_REF:0000120 | ACCEPT | Summary: Vapar_2982 (C5CNX5) is a YggX-family Fe(2+)-trafficking protein retaining the essential Cys7 residue required for intracellular Fe(2+) binding. Reason: Vapar_2982 (C5CNX5) is a conserved 90-residue YggX-family Fe(2+)-trafficking protein (HAMAP MF_00686, InterPro IPR007457) whose sequence (MARMVQCIKL...) retains the invariant Cys7 residue shown in Salmonella enterica YggX (PMID:12670952) to be essential for Fe(2+) trafficking and decreasing chelatable Fe(2+) in solution. Supporting Evidence: UniProtKB:C5CNX5 CC -!- FUNCTION: Could be a mediator in iron transactions between iron CC acquisition and iron-requiring processes, such as synthesis and/or CC repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP- CC Rule:MF_00686}. PMID:12670952 The ability of purified YggX to protect DNA from Fenton chemistry mediated damage in vitro and to decrease the concentration of Fe(II) ions in solution available for chelation provided a framework for the interpretation of data obtained from in vivo experiments. PMID:12670952 The interpretation of in vitro assay results, within the context of the in vivo phenotypes, was validated by a mutant variant of YggX (C7S) that was unable to function in vivo or in vitro. |
| GO:0005829 cytosol | IEA GO_REF:0000118 | ACCEPT | Reason: YggX-family Fe(2+)-trafficking proteins (IPR007457 / HAMAP MF_00686) are soluble cytoplasmic proteins lacking signal peptides or transmembrane helices. Supporting Evidence: UniProtKB:C5CNX5 DR InterPro; IPR007457; Fe_traffick_prot_YggX. |
| GO:0034599 cellular response to oxidative stress | IEA GO_REF:0000118 | KEEP AS NON CORE | Summary: Retained as non-core cellular phenotype: YggX-family Fe(II)-trafficking proteins protect cells against superoxide and Fenton-mediated hydroxyl radical stress (PMID:11416172, PMID:12670952). Reason: Protection against oxidative stress (GO:0034599) is a downstream cellular phenotype resulting from YggX-mediated cytosolic Fe(II) sequestration and [Fe-S] cluster protection, characterized experimentally in Salmonella enterica YggX (PMID:11416172, PMID:12670952) and propagated to Vapar_2982 via TreeGrafter (PANTHER:PTN002863974); retained as non-core. Supporting Evidence: PMID:12670952 The ability of purified YggX to protect DNA from Fenton chemistry mediated damage in vitro and to decrease the concentration of Fe(II) ions in solution available for chelation provided a framework for the interpretation of data obtained from in vivo experiments. PMID:11416172 Here it is shown that elevated levels of the YggX protein increase the resistance of Salmonella enterica to superoxide stress, reverse enzymatic defects attributed to oxidized [Fe-S] clusters, and decrease the spontaneous mutation frequency. UniProtKB:C5CNX5 DR PANTHER; PTHR36965:SF1; FE(2+)-TRAFFICKING PROTEIN-RELATED; 1. |
| GO:0006879 intracellular iron ion homeostasis | ISS PMID:12670952 The YggX protein of Salmonella enterica is involved in Fe(II... | NEW | Reason: Inferred from sequence similarity (ISS) to experimentally characterized Salmonella enterica YggX (PMID:12670952, PMID:11416172), together with HAMAP rule MF_00686 (InterPro IPR007457), which annotates Vapar_2982 (PE 3, Probable Fe(2+)-trafficking protein) as a candidate mediator in intracellular iron transactions between iron acquisition and Fe-S cluster synthesis or repair; Vapar_2982 (MARMVQCIKL...) retains the invariant Cys7 residue essential for YggX Fe(II)-trafficking activity in vivo and in vitro. Supporting Evidence: PMID:12670952 The ability of purified YggX to protect DNA from Fenton chemistry mediated damage in vitro and to decrease the concentration of Fe(II) ions in solution available for chelation provided a framework for the interpretation of data obtained from in vivo experiments. PMID:12670952 The interpretation of in vitro assay results, within the context of the in vivo phenotypes, was validated by a mutant variant of YggX (C7S) that was unable to function in vivo or in vitro. PMID:11416172 Here it is shown that elevated levels of the YggX protein increase the resistance of Salmonella enterica to superoxide stress, reverse enzymatic defects attributed to oxidized [Fe-S] clusters, and decrease the spontaneous mutation frequency. UniProtKB:C5CNX5 CC -!- FUNCTION: Could be a mediator in iron transactions between iron CC acquisition and iron-requiring processes, such as synthesis and/or CC repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP- CC Rule:MF_00686}. |
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Download this section (compressed HTML)Q: How is expression of Vapar_2982 (yggX/fetP) coordinated with OxyR, SoxR, and Fur regulons during rhizosphere oxidative bursts or heavy-metal exposure in Variovorax paradoxus S110?
Experiment: Construct a delta-Vapar_2982 deletion mutant in Variovorax paradoxus S110 and assay aconitase [4Fe-4S] activity and paraquat/hydrogen peroxide sensitivity relative to wild-type.
Hypothesis: Loss of Vapar_2982 increases labile cytosolic Fe(2+) damage to [4Fe-4S] dehydratases under superoxide or peroxide stress.
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