The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The UniProt entry C5B1I2 from Methylorubrum extorquens AM1 is annotated as FecR, an iron siderophore sensor. In the retrieved literature, no primary paper explicitly maps the gene symbol “mluR” or locus MexAM1_META1p4130 to an experimentally characterized protein; thus, “mluR” is ambiguous/under-cited for this organism in accessible full text. Functional annotation is therefore best supported by conserved domain architecture and the strongly established mechanism of FecR-like cell-surface signaling (CSS) anti-σ/pro-σ factors (inner-membrane, periplasm-to-cytoplasm transducers), plus recent 2023–2024 mechanistic updates in CSS systems. (braun2022transcriptionregulationof pages 13-13, braun2022transcriptionregulationof pages 2-3)
In current understanding, FecR-family proteins are membrane-anchored transducers that couple TonB-dependent outer-membrane receptors (that detect ferric-citrate or siderophore-like signals) to cytoplasmic extracytoplasmic-function (ECF) σ factors, thereby inducing transcription of uptake/transport genes; activation often involves regulated, sequential proteolysis (Prc/CtpA-family periplasmic proteases and the intramembrane protease RseP). (braun2022transcriptionregulationof pages 2-3, braun2022transcriptionregulationof pages 9-10, braun2022transcriptionregulationof pages 5-6)
Target protein (given): UniProt C5B1I2, described as FecR, iron siderophore sensor protein, in Methylorubrum extorquens strain AM1 (ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133). The listed domains (InterPro/Pfam) include FecR, FecR_N, and a Ferric-dicitrate sensor transmembrane module, consistent with a FecR-like CSS transducer. (braun2022transcriptionregulationof pages 2-3)
Across the retrieved full-text sources (reviews and primary research), no direct mention was found linking the gene symbol mluR to C5B1I2 / MexAM1_META1p4130, nor describing this specific locus experimentally. Accordingly:
CSS is an envelope-spanning regulatory mechanism in which outer-membrane TonB-dependent receptors detect extracellular metal complexes (e.g., ferric citrate or siderophores) and transmit signals into the cytoplasm to activate transcription of uptake genes. The canonical example is the E. coli Fec system, composed of:
Ligand binding to the receptor’s extracellular side triggers conformational changes reaching the periplasmic signaling domain, which interacts with the periplasmic portion of FecR; FecR then controls FecI activity. (braun2022transcriptionregulationof pages 2-3)
FecR-family proteins are often described as anti-σ (sequestering an ECF σ factor) and/or pro-σ (generating an activating σ-binding fragment) regulators. Mechanistically, a defining feature is that the output (σ activation) is mediated by an N-terminal cytosolic region of FecR-like proteins that physically interacts with and stimulates the partner ECF σ factor (e.g., binding σ4). (braun2022transcriptionregulationof pages 5-6, braun2022transcriptionregulationof pages 6-7)
For C5B1I2 (FecR-like), the primary function is not catalysis or transport. Rather, the protein’s function is signal transduction and transcriptional regulation: coupling extracellular iron-carrier availability to transcriptional activation of transport/uptake systems via an ECF σ factor. (braun2022transcriptionregulationof pages 2-3, braun2022transcriptionregulationof pages 5-6)
Because AM1-specific experiments for C5B1I2 were not retrieved, the following annotation is best supported as high-confidence inference from conserved FecR-family features.
The FecR archetype is an inner-membrane protein with:
This topology strongly supports that C5B1I2 functions at the cytoplasmic membrane and in the periplasmic space (signal reception), while regulating transcription in the cytoplasm through σ factor control. (braun2022transcriptionregulationof pages 5-6, braun2022transcriptionregulationof pages 6-7)
Canonical CSS logic (applicable template for C5B1I2):
In E. coli, this specifically controls fecA and related genes; iron-responsive repression is commonly integrated via Fur. (braun2022transcriptionregulationof pages 2-3, braun2022transcriptionregulationof pages 10-10)
A major characteristic of FecR-like proteins is regulated intramembrane proteolysis (RIP). In the canonical model:
Multiple fragment sizes are reported for FecR-like processing, including ~20, 15, and 12 kDa species. (braun2022transcriptionregulationof pages 9-10, braun2022transcriptionregulationof pages 5-6)
Genetic mapping in FecR indicates the activating region is near residues ~1–59, and specific conserved residues (e.g., L13, W19, W39, W50 in the model) are critical for induction. This supports annotation of C5B1I2 N-terminus as the σ-factor binding/activating module, with the periplasmic domain acting as the sensor-input module. (braun2022transcriptionregulationof pages 6-7)
A 2024 study in Pseudomonas aeruginosa (Fox system) provides a major conceptual update: the TonB-dependent receptor signaling domain can already bind the anti-σ factor in the absence of ligand, and this interaction can protect the anti-σ factor from proteolysis, suppressing σECF activation. Ligand-dependent changes then permit proteolytic activation. This revises the older “signal promotes binding” view into a model where signal relieves a protected state, enabling degradation/activation. (wettstadt2024bacterialtonbdependenttransducers pages 2-3, wettstadt2024bacterialtonbdependenttransducers pages 1-2)
The same study provides residue-level evidence for a structured receptor–anti-σ interface (β-sheet interface; key residues) and shows receptor processing (FoxA ~84–85 kDa vs a processed ~73–74 kDa form), reinforcing that CSS can involve coordinated processing of multiple envelope proteins. (wettstadt2024bacterialtonbdependenttransducers pages 10-12, wettstadt2024bacterialtonbdependenttransducers media 7647bb29, wettstadt2024bacterialtonbdependenttransducers media b827a8a5)
A 2023 mBio study summarizes key mechanistic features of RseP (S2P-family intramembrane protease) and notes its role in cleaving FecR-type substrates, with structural elements (PDZ domains as a filter; membrane-reentrant β-sheet near the active site) helping explain substrate selection and intramembrane cleavage. These advances strengthen the mechanistic plausibility that a FecR-like AM1 protein would be regulated by conserved RIP machinery. (yokoyama2023s2pintramembraneprotease pages 1-2)
Even though these values are derived from model systems (primarily E. coli Fec), they provide quantitative constraints consistent with a FecR-family annotation:
For 2024 CSS updates:
Direct AM1 literature evidence for C5B1I2 is missing in retrieved sources, but Methylorubrum extorquens AM1 clearly deploys TonB-dependent systems for metal acquisition (well documented for lanthanides), and related methylobacteria use siderophore-like metallophores for iron/lanthanide availability.
Work in M. extorquens AM1 describes a lanthanide uptake system involving TonB-dependent receptors (e.g., LutH) and downstream transport components, in a manner explicitly compared to siderophore-mediated Fe uptake. This confirms AM1’s envelope is equipped for TonB-dependent, metallophore-like acquisition, which is the same architectural context required for a FecR-like iron-sensor transducer. (zytnick2022discoveryandcharacterization pages 1-3, roszczenkojasinska2019lanthanidetransportstorage pages 5-8)
Lanthanide acquisition by methylotrophs is motivating for biotechnological recovery of lanthanides from waste streams; AM1 lanthanide uptake and storage are discussed as a step toward designing sustainable recovery platforms. (zytnick2022discoveryandcharacterization pages 1-3)
A lanthanophore (methylolanthanin) is described as enabling normal lanthanide accumulation, with overexpression increasing bioaccumulation, and environmental lanthanide concentrations in phyllosphere are reported (0.7–7 μg/g dry weight), contextualizing bioavailability challenges that metallophore systems address. (zytnick2022discoveryandcharacterization pages 1-3)
In Methylobacterium aquaticum strain 22A, a staphyloferrin B-like siderophore cluster is required for growth under low iron; the siderophore also solubilizes insoluble lanthanide oxide and is linked to methanol growth, and multiple TonB-dependent receptors are implicated in iron-citrate and lanthanide uptake. This supports the ecological plausibility of an iron-sensing CSS regulator in methylobacteria and provides an implementation model for how metallophore pathways can integrate Fe and Ln physiology. (juma2022siderophoreforlanthanide pages 1-2, juma2022siderophoreforlanthanide pages 9-10)
The most authoritative synthesis used here is the 2022 FEMS Microbiology Reviews article, which presents FecR-type proteins as a mechanistically defined class: envelope-spanning, membrane-anchored regulators that activate ECF σ factors via proteolytic cascades initiated by TonB-dependent receptor signaling. This review is widely consistent with (and conceptually extended by) 2024 findings showing receptor–anti-σ interactions can be protective in the absence of signal. (braun2022transcriptionregulationof pages 5-6, wettstadt2024bacterialtonbdependenttransducers pages 2-3)
| Annotation aspect | Evidence / finding | Interpretation for UniProt C5B1I2 (MexAM1_META1p4130, putative mluR) | Evidence source (citation id) |
|---|---|---|---|
| Identity verification status | No direct literature mapping found in retrieved sources for the symbol mluR, locus MexAM1_META1p4130/META1p4130, or direct experimental characterization of UniProt C5B1I2 in Methylorubrum extorquens AM1. | The symbol is ambiguous/under-cited; functional annotation should therefore be based on the UniProt assignment and conserved FecR-family architecture/mechanism, while avoiding conflation with unrelated genes of similar name. | (braun2022transcriptionregulationof pages 13-13, braun2022transcriptionregulationof pages 2-3) |
| UniProt-provided identity | UniProt identifies C5B1I2 as FecR, iron siderophore sensor protein from Methylorubrum extorquens AM1, locus MexAM1_META1p4130, with domains IPR006860 FecR, IPR032623 FecR_N, IPR012373 Ferrdict_sens_TM, PF16220 DUF4880, PF04773 FecR. | The domain set is consistent with a FecR-like anti-σ/pro-σ transducer that links an outer-membrane TonB-dependent receptor signal to cytoplasmic transcriptional control of iron uptake genes. | (braun2022transcriptionregulationof pages 2-3) |
| Canonical protein class | FecR-like proteins are membrane-embedded regulatory proteins in TonB-dependent cell-surface signaling (CSS) systems, working with an outer-membrane receptor (e.g., FecA) and an ECF σ factor (e.g., FecI). | C5B1I2 is best interpreted as the inner-membrane signaling/anti-σ component of a CSS pathway, not as an enzyme or transporter. | (braun2022transcriptionregulationof pages 2-3) |
| Inferred cellular localization / topology | Archetypal FecR has an N-proximal cytoplasmic region, a single transmembrane helix near residues ~85–100 (prediction centered around ~82–100), and a C-proximal periplasmic domain that contacts the receptor signaling domain. | For C5B1I2, the most likely topology is cytoplasmic N-terminus → single inner-membrane TM → periplasmic C-terminus. | (braun2022transcriptionregulationof pages 5-6, braun2022transcriptionregulationof pages 6-7) |
| Periplasmic interaction partner | In the Fec archetype, the outer-membrane receptor signaling domain (FecA residues 1–79) binds the periplasmic domain of FecR (residues 101–317); related PupB:PupR proteins form a stable 1:1 periplasmic signaling complex. | C5B1I2 is predicted to receive signal from a TonB-dependent outer-membrane transducer/receptor via its periplasmic C-terminal region. | (braun2022transcriptionregulationof pages 5-6, braun2022transcriptionregulationof pages 4-5) |
| Cytoplasmic output function | The FecR N-terminus directly stimulates the partner ECF σ factor; induction-competent region maps to about residues 1–59 (or 9–59) in the model system, and short N-terminal fragments can be sufficient for activation. | C5B1I2 likely functions by controlling an ECF σ factor in the cytoplasm, rather than binding DNA directly. | (braun2022transcriptionregulationof pages 6-7, braun2022transcriptionregulationof pages 13-13) |
| Pathway role | Canonical pathway: TonB-dependent receptor ligand binding → conformational signaling across the envelope → FecR-like anti-σ processing → ECF σ activation → transcription of iron uptake genes. Fur commonly represses these systems under iron sufficiency. | C5B1I2 is most plausibly part of an iron-responsive transcriptional signaling pathway for uptake functions, likely downstream of a TonB-dependent receptor and upstream of iron acquisition gene expression. | (braun2022transcriptionregulationof pages 2-3, braun2022transcriptionregulationof pages 10-10) |
| Proteolytic activation mechanism | FecR-like proteins undergo regulated intramembrane proteolysis: periplasmic cleavage(s) generate intermediates, then RseP cleaves within/near the membrane to release an N-terminal activating fragment. Prc acts upstream in the periplasm; newer CSS work also implicates CtpA in some systems. | C5B1I2 is expected to be a proteolytically activated transducer, not a static scaffold. | (braun2022transcriptionregulationof pages 9-10, braun2022transcriptionregulationof pages 8-9, yokoyama2023s2pintramembraneprotease pages 1-2, wettstadt2024bacterialtonbdependenttransducers pages 2-3) |
| Fragment sizes / processing statistics | Reported FecR-related fragments include approximately 20 kDa, 15 kDa, and 12 kDa products; additional species around 25 kDa and 17 kDa are described in related analyses, with FecR85 comigrating near the 15-kDa form. | These fragment sizes provide a benchmark for interpreting any future immunoblot/proteolysis experiments on C5B1I2. | (braun2022transcriptionregulationof pages 9-10, braun2022transcriptionregulationof pages 5-6, braun2022transcriptionregulationof pages 8-9, braun2022transcriptionregulationof pages 13-13) |
| Key functional residues in activating N-terminus | In E. coli FecR, mutations L13Q, W19R, W39R, W50R in the N-terminal activating region abolish induction, and these residues are conserved in FecR-like proteins. | Conserved N-terminal residues in C5B1I2 would be strong candidates for σ-factor interaction and activation. | (braun2022transcriptionregulationof pages 6-7) |
| Quantitative regulatory data | Unrepressed FecI abundance is <1 molecule/cell in the model system; in an rseP mutant, fecA-lacZ is not induced by ferric citrate, whereas wild type shows about 10-fold induction. | These values indicate that FecR/RseP-dependent signaling can strongly gate transcription and that σ-factor abundance is normally extremely low. | (braun2022transcriptionregulationof pages 5-6, braun2022transcriptionregulationof pages 9-10) |
| Recent 2024 mechanistic update | In the Fox CSS system, the receptor signaling domain can bind the anti-σ factor before induction and protect it from proteolysis; this revises the older view that receptor–anti-σ contact occurs only after ligand detection. | For C5B1I2, the resting state may involve a preformed protected receptor–anti-σ complex rather than a purely signal-triggered first contact. | (wettstadt2024bacterialtonbdependenttransducers pages 2-3, wettstadt2024bacterialtonbdependenttransducers pages 1-2) |
| Residue-level interface data from 2024 | AlphaFold-guided and mutational analysis in FoxA/FoxR identified a 5-stranded β-sheet interface; FoxR S292/G293 and FoxA S81 are critical for interaction, while β-strand-disrupting substitutions abolish binding. | Although from a different bacterium, these data support a conserved structured periplasmic receptor–anti-σ interface relevant to C5B1I2 domain-function inference. | (wettstadt2024bacterialtonbdependenttransducers pages 10-12, wettstadt2024bacterialtonbdependenttransducers media b827a8a5) |
| Receptor processing benchmark | In the Fox system, Western blots show full-length FoxA ~84–85 kDa and a processed form lacking the signaling domain at ~73–74 kDa. | These data reinforce that CSS regulation can involve processing of both the anti-σ protein and the receptor, which may be relevant when interpreting future C5B1I2-associated receptor studies. | (wettstadt2024bacterialtonbdependenttransducers pages 10-12, wettstadt2024bacterialtonbdependenttransducers media 7647bb29) |
| Methylorubrum-specific context | M. extorquens AM1 has documented TonB-dependent metal uptake systems (e.g., lanthanide uptake via LutH and a TonB-ABC pathway), but retrieved sources did not directly connect these methylotroph studies to a named FecR/FecI-like iron CSS module or to mluR/C5B1I2. | The organism clearly uses TonB-dependent metal acquisition, making a FecR-like iron signaling protein biologically plausible, but direct experimental evidence for C5B1I2 remains absent in retrieved literature. | (zytnick2022discoveryandcharacterization pages 1-3) |
Table: This table consolidates the strongest available evidence for annotating UniProt C5B1I2 as a FecR-like inner-membrane anti-sigma/sensor protein in Methylorubrum extorquens AM1. It distinguishes direct evidence from inference, highlights the ambiguity around the symbol mluR, and maps each claim to citation-ready context IDs.
| Year | System/organism | Key finding | Why it matters for annotating M. extorquens AM1 mluR (C5B1I2) | Publication (with URL) | Evidence source (pqac id) |
|---|---|---|---|---|---|
| 2024 | Fox cell-surface signaling system, Pseudomonas aeruginosa | The TonB-dependent transducer signaling domain (FoxA SD) binds the anti-σ factor FoxR before induction and protects it from proteolysis; this revises the classical model in which receptor–anti-σ contact was thought to occur mainly after ligand sensing. | Suggests C5B1I2, if truly FecR-like, may exist in a preformed receptor-bound resting complex rather than acting only after siderophore/iron signal arrival. This supports annotation as a regulated signaling transducer, not merely a passive anti-σ factor. | Wettstadt et al. 2024, PLOS Biology (published Dec 2024). https://doi.org/10.1371/journal.pbio.3002920 | (wettstadt2024bacterialtonbdependenttransducers pages 2-3, wettstadt2024bacterialtonbdependenttransducers pages 1-2) |
| 2024 | Fox/FoxR interface, Pseudomonas aeruginosa | AlphaFold-guided and mutational analysis identified a structured 5-stranded β-sheet interface between the receptor signaling domain and anti-σ factor; residues FoxR S292/G293 and FoxA S81 are critical for interaction. | Strengthens inference that the periplasmic domain of C5B1I2 should mediate specific receptor coupling through an ordered interface, consistent with UniProt/IPR assignment to the FecR family. | Wettstadt et al. 2024, PLOS Biology (published Dec 2024). https://doi.org/10.1371/journal.pbio.3002920 | (wettstadt2024bacterialtonbdependenttransducers pages 10-12, wettstadt2024bacterialtonbdependenttransducers media b827a8a5) |
| 2024 | Fox CSS proteolysis, Pseudomonas aeruginosa | Periplasmic proteases Prc and CtpA differentially control anti-σ factor turnover: Δprc stabilizes FoxR C-terminal fragments, whereas ΔctpA lowers FoxR C-terminal abundance; FoxA itself is also proteolytically processed. | Indicates that annotation of C5B1I2 should include likely participation in a multi-step proteolytic control pathway, potentially involving both anti-σ processing and receptor processing. | Wettstadt et al. 2024, PLOS Biology (published Dec 2024). https://doi.org/10.1371/journal.pbio.3002920 | (wettstadt2024bacterialtonbdependenttransducers pages 2-3, wettstadt2024bacterialtonbdependenttransducers pages 10-12, wettstadt2024bacterialtonbdependenttransducers media 7647bb29) |
| 2023 | RseP intramembrane proteolysis, Escherichia coli | RseP, an S2P-family intramembrane protease, is confirmed as a protease that cleaves FecR-type membrane substrates; recent structural work highlights tandem PDZ domains as a size-exclusion filter and a membrane-reentrant β-sheet that helps discriminate substrates. | Supports a mechanistic annotation for C5B1I2 as a likely substrate of regulated intramembrane proteolysis after prior periplasmic trimming, a hallmark of FecR-family signaling proteins. | Yokoyama et al. 2023, mBio (published Jul 2023). https://doi.org/10.1128/mbio.01086-23 | (yokoyama2023s2pintramembraneprotease pages 1-2) |
| 2023 | TonB-dependent outer-membrane transport/signaling review, mainly Gram-negative bacteria | Updated review of TonB/ExbB/ExbD energization emphasizes that conformational changes in TonB-dependent receptors can alter interactions with periplasmic anti-σ partners and thereby affect transcriptional signaling. | Reinforces that a FecR annotation for C5B1I2 implies coupling to a TonB-dependent outer-membrane receptor and envelope-spanning signal transduction rather than transport or catalysis by C5B1I2 itself. | Braun et al. 2023, Journal of Bacteriology (published Jun 2023). https://doi.org/10.1128/jb.00035-23 | (wettstadt2024bacterialtonbdependenttransducers pages 2-3) |
| 2022 (background) | Canonical Fec system, mainly E. coli and related Gram-negative bacteria | FecR-like proteins are inner-membrane anti-/pro-σ factors with cytoplasmic N-termini, a single transmembrane helix around residues ~85–100, and periplasmic C-termini that receive receptor signals; activation proceeds through sequential cleavage yielding ~20, 15, and 12 kDa fragments, with RseP acting late in the cascade. | This remains the best-supported mechanistic template for annotating C5B1I2 in the absence of direct AM1 experiments: a membrane-anchored FecR-like sensor transmitting iron uptake signals to an ECF σ factor. | Braun et al. 2022, FEMS Microbiology Reviews (published Feb 2022). https://doi.org/10.1093/femsre/fuac010 | (braun2022transcriptionregulationof pages 5-6, braun2022transcriptionregulationof pages 13-13, braun2022transcriptionregulationof pages 9-10) |
Table: This table summarizes the most relevant 2023–2024 advances in FecR-like anti-sigma factor biology and regulated intramembrane proteolysis. It helps anchor the annotation of Methylorubrum extorquens AM1 C5B1I2 in current mechanistic understanding while clearly separating direct evidence from inference.
The following figure panels provide direct visual support for the updated CSS model (receptor/anti-σ interface; receptor processing) that informs modern annotation of FecR-like proteins:
Proposed primary function: C5B1I2 is most plausibly a FecR-family inner-membrane signal transducer (anti-σ/pro-σ regulator) that couples an extracellular iron-carrier signal sensed by a TonB-dependent outer-membrane receptor to activation of an ECF σ factor, inducing transcription of iron uptake/transport genes. (braun2022transcriptionregulationof pages 2-3, braun2022transcriptionregulationof pages 5-6)
Likely localization: inner (cytoplasmic) membrane with an N-terminal cytosolic region (σ-factor interaction) and a C-terminal periplasmic sensing/interface domain; signal transduction spans periplasm-to-cytoplasm. (braun2022transcriptionregulationof pages 5-6, braun2022transcriptionregulationof pages 6-7)
Mechanistic hallmark: activation by a proteolytic cascade (periplasmic proteases such as Prc/CtpA-type plus intramembrane RseP) generating characteristic N-terminal fragments that activate σ factors; 2024 evidence supports that receptor–anti-σ binding may also serve to protect the anti-σ from proteolysis until the inducing ligand is present. (braun2022transcriptionregulationof pages 9-10, wettstadt2024bacterialtonbdependenttransducers pages 2-3)
References
(braun2022transcriptionregulationof pages 13-13): Volkmar Braun, Marcus D Hartmann, and Klaus Hantke. Transcription regulation of iron carrier transport genes by ecf sigma factors through signaling from the cell surface into the cytoplasm. FEMS Microbiology Reviews, Feb 2022. URL: https://doi.org/10.1093/femsre/fuac010, doi:10.1093/femsre/fuac010. This article has 12 citations and is from a domain leading peer-reviewed journal.
(braun2022transcriptionregulationof pages 2-3): Volkmar Braun, Marcus D Hartmann, and Klaus Hantke. Transcription regulation of iron carrier transport genes by ecf sigma factors through signaling from the cell surface into the cytoplasm. FEMS Microbiology Reviews, Feb 2022. URL: https://doi.org/10.1093/femsre/fuac010, doi:10.1093/femsre/fuac010. This article has 12 citations and is from a domain leading peer-reviewed journal.
(braun2022transcriptionregulationof pages 9-10): Volkmar Braun, Marcus D Hartmann, and Klaus Hantke. Transcription regulation of iron carrier transport genes by ecf sigma factors through signaling from the cell surface into the cytoplasm. FEMS Microbiology Reviews, Feb 2022. URL: https://doi.org/10.1093/femsre/fuac010, doi:10.1093/femsre/fuac010. This article has 12 citations and is from a domain leading peer-reviewed journal.
(braun2022transcriptionregulationof pages 5-6): Volkmar Braun, Marcus D Hartmann, and Klaus Hantke. Transcription regulation of iron carrier transport genes by ecf sigma factors through signaling from the cell surface into the cytoplasm. FEMS Microbiology Reviews, Feb 2022. URL: https://doi.org/10.1093/femsre/fuac010, doi:10.1093/femsre/fuac010. This article has 12 citations and is from a domain leading peer-reviewed journal.
(braun2022transcriptionregulationof pages 6-7): Volkmar Braun, Marcus D Hartmann, and Klaus Hantke. Transcription regulation of iron carrier transport genes by ecf sigma factors through signaling from the cell surface into the cytoplasm. FEMS Microbiology Reviews, Feb 2022. URL: https://doi.org/10.1093/femsre/fuac010, doi:10.1093/femsre/fuac010. This article has 12 citations and is from a domain leading peer-reviewed journal.
(braun2022transcriptionregulationof pages 10-10): Volkmar Braun, Marcus D Hartmann, and Klaus Hantke. Transcription regulation of iron carrier transport genes by ecf sigma factors through signaling from the cell surface into the cytoplasm. FEMS Microbiology Reviews, Feb 2022. URL: https://doi.org/10.1093/femsre/fuac010, doi:10.1093/femsre/fuac010. This article has 12 citations and is from a domain leading peer-reviewed journal.
(wettstadt2024bacterialtonbdependenttransducers pages 2-3): Sarah Wettstadt, Francisco J. Marcos-Torres, Joaquín R. Otero-Asman, Alicia García-Puente, Álvaro Ortega, and María A. Llamas. Bacterial tonb-dependent transducers interact with the anti-σ factor in absence of the inducing signal protecting it from proteolysis. Dec 2024. URL: https://doi.org/10.1371/journal.pbio.3002920, doi:10.1371/journal.pbio.3002920. This article has 1 citations and is from a highest quality peer-reviewed journal.
(wettstadt2024bacterialtonbdependenttransducers pages 1-2): Sarah Wettstadt, Francisco J. Marcos-Torres, Joaquín R. Otero-Asman, Alicia García-Puente, Álvaro Ortega, and María A. Llamas. Bacterial tonb-dependent transducers interact with the anti-σ factor in absence of the inducing signal protecting it from proteolysis. Dec 2024. URL: https://doi.org/10.1371/journal.pbio.3002920, doi:10.1371/journal.pbio.3002920. This article has 1 citations and is from a highest quality peer-reviewed journal.
(wettstadt2024bacterialtonbdependenttransducers pages 10-12): Sarah Wettstadt, Francisco J. Marcos-Torres, Joaquín R. Otero-Asman, Alicia García-Puente, Álvaro Ortega, and María A. Llamas. Bacterial tonb-dependent transducers interact with the anti-σ factor in absence of the inducing signal protecting it from proteolysis. Dec 2024. URL: https://doi.org/10.1371/journal.pbio.3002920, doi:10.1371/journal.pbio.3002920. This article has 1 citations and is from a highest quality peer-reviewed journal.
(wettstadt2024bacterialtonbdependenttransducers media 7647bb29): Sarah Wettstadt, Francisco J. Marcos-Torres, Joaquín R. Otero-Asman, Alicia García-Puente, Álvaro Ortega, and María A. Llamas. Bacterial tonb-dependent transducers interact with the anti-σ factor in absence of the inducing signal protecting it from proteolysis. Dec 2024. URL: https://doi.org/10.1371/journal.pbio.3002920, doi:10.1371/journal.pbio.3002920. This article has 1 citations and is from a highest quality peer-reviewed journal.
(wettstadt2024bacterialtonbdependenttransducers media b827a8a5): Sarah Wettstadt, Francisco J. Marcos-Torres, Joaquín R. Otero-Asman, Alicia García-Puente, Álvaro Ortega, and María A. Llamas. Bacterial tonb-dependent transducers interact with the anti-σ factor in absence of the inducing signal protecting it from proteolysis. Dec 2024. URL: https://doi.org/10.1371/journal.pbio.3002920, doi:10.1371/journal.pbio.3002920. This article has 1 citations and is from a highest quality peer-reviewed journal.
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