FecR-family inner-membrane signal transducer (anti-sigma/pro-sigma factor) of a TonB-dependent cell-surface signaling (CSS) system. By conserved domain architecture (InterPro FecR/FecR_N + ferric-dicitrate sensor TM module; Pfam PF04773 FecR, PF16220 DUF4880) the protein is predicted to couple an outer-membrane TonB-dependent receptor signal to an extracytoplasmic-function (ECF) sigma factor, controlling transcription of metal-uptake/transport genes. A more specific role as the anti-sigma regulator of the putative mluA/mluR/mluI lanthanide-acquisition operon (sequestering an ECF sigma factor MluI) has been proposed, but no primary literature directly characterizes this locus (C5B1I2 / MexAM1_META1p4130) experimentally; the lanthanide/MluI specifics remain inferential.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0016989 sigma factor antagonist activity | IEA GO_REF:0000118 | ACCEPT | Summary: Consistent with the FecR-family identity. FecR-family proteins are membrane-anchored anti-sigma/pro-sigma transducers that sequester or otherwise control an ECF sigma factor; the conserved domain architecture (FecR/FecR_N) supports sigma factor antagonist activity as the molecular function. The specific cognate sigma factor (proposed to be a lanthanide-responsive MluI) is not experimentally established for this locus. Supporting Evidence: file:METEA/mluR/mluR-deep-research-falcon.md FecR-family proteins are often described as **anti-ฯ** (sequestering an ECF ฯ factor) file:METEA/mluR/mluR-deep-research-falcon.md most plausibly a **FecR-family inner-membrane signal transducer (anti-ฯ/pro-ฯ regulator)** |
| GO:0045892 negative regulation of DNA-templated transcription | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: Plausible as the downstream consequence of sigma factor antagonism - by sequestering its cognate ECF sigma factor, the protein prevents that sigma factor from directing RNA polymerase to target promoters, so transcription of the target uptake regulon is repressed under non-inducing conditions. mluR does not bind DNA itself; the regulatory output is mediated through the sigma factor. Retained as a non-core, inferred consequence of the anti-sigma molecular function. Supporting Evidence: file:METEA/mluR/mluR-deep-research-falcon.md C5B1I2 likely functions by **controlling an ECF ฯ factor in the cytoplasm**, rather than binding DNA directly |
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