TonB-dependent outer membrane receptor (locus MexAM1_META1p4129) of the TonB-dependent receptor family. Reported as mluA (methylolanthanin uptake A) within the mll cluster, functioning in active uptake of a lanthanide-metallophore (methylolanthanin) complex across the outer membrane into the periplasm, and as a cell-surface signaling receptor that couples to the anti-sigma factor MluR. Note that primary-literature retrieval for the bare accession C5B1I1 is sparse and the family-level mechanism (outer-membrane, TonB/ExbB/ExbD-energized uptake of a scarce metal-chelate substrate delivered to the periplasm) is the most robustly supported function; the specific lanthanide-metallophore substrate assignment rests on the mll-cluster characterization.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006826 iron ion transport | IEA GO_REF:0000043 | REMOVE | Summary: Incorrect substrate. This TonB-dependent receptor is not an iron transporter; it is implicated in uptake of a lanthanide-metallophore complex, and even at the family level the substrate of this specific accession cannot be assigned as iron. The keyword-derived iron transport annotation reflects generic TonB/siderophore-family inference, not iron specificity. Supporting Evidence: file:METEA/mluA/mluA-deep-research-falcon.md there is no locus-specific genetic/biochemical evidence in the retrieved corpus identifying the precise ligand for UniProt C5B1I1 in AM1 |
| GO:0009279 cell outer membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Correct. As a TonB-dependent receptor of the TonB-dependent receptor family, the protein is an integral outer membrane beta-barrel transporter. Both deep-research sources concur on outer-membrane localization, consistent with the UniProt subcellular location annotation. Supporting Evidence: file:METEA/mluA/mluA-deep-research-falcon.md Thus C5B1I1 should be localized to the file:METEA/mluA/mluA-deep-research-perplexity.md the protein is an integral outer membrane protein with the characteristic 22-stranded Ξ²-barrel structure typical of this protein family |
| GO:0015343 siderophore-iron transmembrane transporter activity | IEA GO_REF:0000002 | MODIFY | Summary: Wrong specificity but correct general activity. The protein is a TonB-dependent active uptake transporter, but the substrate is a lanthanide-metallophore, not an iron-siderophore. Rather than removing the transporter activity outright, generalize to transmembrane transporter activity (the iron-siderophore reaction defined for this term does not apply). The family-level uptake-transporter function is well supported; the precise ligand is not iron. Proposed replacements: transmembrane transporter activity Supporting Evidence: file:METEA/mluA/mluA-deep-research-falcon.md C5B1I1 most likely functions as an file:METEA/mluA/mluA-deep-research-falcon.md the substrate should be reported as |
| GO:0015344 siderophore uptake transmembrane transporter activity | IEA GO_REF:0000118 | MODIFY | Summary: Wrong specificity but correct general activity. The TreeGrafter-propagated iron-siderophore uptake term over-specifies the substrate. The protein performs TonB-energized active uptake transport, but of a lanthanide-metallophore rather than an iron-siderophore; generalize to transmembrane transporter activity. Proposed replacements: transmembrane transporter activity Supporting Evidence: file:METEA/mluA/mluA-deep-research-falcon.md they mediate uptake of substrates |
| GO:0015891 siderophore transport | IEA GO_REF:0000002 | REMOVE | Summary: Incorrect specificity. Siderophore transport is defined as movement of low-molecular-weight Fe(III)-chelating substances. This receptor is implicated in uptake of a lanthanide-metallophore complex (methylolanthanin), not an Fe(III) siderophore, so the term is inappropriate as an over-specific substrate assignment. Supporting Evidence: file:METEA/mluA/mluA-deep-research-falcon.md the substrate should be reported as |
| GO:0019867 outer membrane | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Correct but less specific than the cell outer membrane annotation. The protein is an outer-membrane TonB-dependent beta-barrel transporter; the Gram-negative cell outer membrane term (GO:0009279) is preferred and is already ACCEPTed and used in core_functions. Keep this broader term as non-core because it is redundant with the more specific GO:0009279 for core representation. Supporting Evidence: file:METEA/mluA/mluA-deep-research-falcon.md Thus C5B1I1 should be localized to the |
| GO:0033214 siderophore-iron import into cell | IEA GO_REF:0000120 | REMOVE | Summary: Incorrect substrate. This term describes import of Fe(III) solubilized by ferric-iron-specific siderophores. The receptor imports a lanthanide-metallophore complex into the periplasm, not siderophore-iron, so the term is inappropriate. Supporting Evidence: file:METEA/mluA/mluA-deep-research-falcon.md there is no locus-specific genetic/biochemical evidence in the retrieved corpus identifying the precise ligand for UniProt C5B1I1 in AM1 |
| GO:0038023 signaling receptor activity | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Plausible and supported. TonB-dependent receptors of this signaling subtype possess an N-terminal signaling (Secretin/TonB short N-terminal) domain; for this protein the mll-cluster work describes a cell-surface signaling system in which the receptor interacts with the anti-sigma factor MluR upon ligand binding. Keep as a non-core signaling-receptor function alongside the core uptake-transport role; the review itself characterizes this as ancillary to the primary metal-chelate uptake-transport function. Supporting Evidence: file:METEA/mluA/mluA-deep-research-perplexity.md The protein contains an N-terminal signaling domain that interacts with the anti-sigma factor MluR, encoded by the adjacent *mluR* gene within the same operon |
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