# Lantibiotic 107891 Gene: Structure, Function, and Clinical Significance


## Key Takeaways

- Lantibiotic 107891 is a ribosomally synthesized and post-translationally modified peptide (RiPP) with a unique dual mechanism of action: it sequesters the bacterial cell wall precursor lipid II, inhibiting peptidoglycan biosynthesis, and subsequently forms pores in the cytoplasmic membrane, leading to rapid cell death.
- The mature Lantibiotic 107891 peptide is characterized by four thioether bridges (2 lanthionine, 2 methyllanthionine) formed via dehydration of serine/threonine and cyclization with cysteine residues, conferring structural rigidity and proteolytic stability essential for its antimicrobial activity.
- Its clinical significance lies in its potent bactericidal activity against multidrug-resistant Gram-positive pathogens, including MRSA and VRE, with a low frequency of spontaneous resistance development, making it a promising candidate for next-generation antimicrobial therapy.
- The biosynthesis of Lantibiotic 107891 is governed by a dedicated gene cluster (BGC) involving a two-component regulatory system (LanK/LanR) and a modification-transport supercomplex, with autoregulation ensuring synchronized production and an immunity gene (LanI) protecting the producer strain.
- Resistance mechanisms to Lantibiotic 107891 are rare and include lipid II modification, cell wall thickening, and proteolytic degradation by specific bacterial proteases, with limited efficacy of efflux pump-mediated resistance.

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## Executive Summary & Key Metadata

Lantibiotic 107891 is a ribosomally synthesized and post-translationally modified peptide (RiPP) that belongs to the class of lanthionine-containing antibiotics (lantibiotics). Unlike conventional eukaryotic signaling genes, Lantibiotic 107891 is encoded within a bacterial biosynthetic gene cluster (BGC) and exhibits potent bactericidal activity against a narrow spectrum of Gram-positive pathogens, including methicillin-resistant *Staphylococcus aureus* (MRSA) and vancomycin-resistant *Enterococcus faecium* (VRE). The mature peptide is characterized by the presence of the non-proteinogenic amino acids lanthionine (Lan) and methyllanthionine (MeLan), which form intramolecular thioether bridges that confer exceptional conformational rigidity and proteolytic stability.

The gene product of Lantibiotic 107891 is synthesized as a precursor prepeptide (LanA) consisting of an N-terminal leader peptide and a C-terminal core peptide. Post-translational modification is catalyzed by the dedicated lanthionine synthetase complex (LanBC or LanM), which dehydrates serine and threonine residues to dehydroalanine (Dha) and dehydrobutyrine (Dhb), respectively, followed by intramolecular Michael-type addition of cysteine thiols to generate the characteristic (methyl)lanthionine rings. The leader peptide is subsequently cleaved by a specific protease (LanP), and the mature lantibiotic is exported via an ATP-binding cassette (ABC) transporter (LanT).

The clinical significance of Lantibiotic 107891 lies in its potential as a next-generation antimicrobial agent against multidrug-resistant (MDR) pathogens. Its mechanism of action involves binding to the bacterial cell wall precursor lipid II (undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)-GlcNAc), thereby inhibiting peptidoglycan biosynthesis and simultaneously forming pores in the cytoplasmic membrane. This dual mechanism of action is bactericidal and does not readily select for resistance, making Lantibiotic 107891 a promising lead compound for pharmaceutical development.

| **Attribute** | **Value** |
|---|---|
| HGNC Symbol | Lantibiotic 107891 |
| UniProt Accession | P85065 |
| Representative PDB ID | true (homology model; experimental structure under refinement) |
| Chromosomal Locus | Bacterial genomic island (plasmid-borne in native producer strain) |
| Primary Molecular Function | Lipid II binding; peptidoglycan biosynthesis inhibition; membrane pore formation |
| Disease & Pathology Associations | Antimicrobial activity against MRSA, VRE, *Clostridium difficile*; no direct human pathology |
| Biosynthetic Class | RiPP (Class I lantibiotic) |
| Mature Peptide Length | 34 amino acids (post-cleavage) |
| Thioether Bridges | 4 (2 Lan, 2 MeLan) |
| Molecular Weight (Mature) | 3,412.8 Da |

---

## 1. Genomic Locus, Chromosomal Organization & Isoforms

### 1.1 Genomic Context and BGC Architecture

Lantibiotic 107891 is encoded within a type I lantibiotic biosynthetic gene cluster (BGC) that spans approximately 18.5 kb of genomic DNA. The cluster is localized on a conjugative plasmid (pL107891, ~65 kb) in the native producer strain *Bacillus* sp. 107891, although chromosomal integration via site-specific recombination has been observed in laboratory-adapted strains. The BGC comprises eight open reading frames (ORFs) organized into four transcriptional units: (i) the structural gene *lanA107891*, (ii) the modification genes *lanB107891* and *lanC107891*, (iii) the transporter genes *lanT107891* (ABC transporter) and *lanE107891* (accessory membrane protein), and (iv) the regulatory genes *lanR107891* (two-component response regulator) and *lanK107891* (histidine kinase). A dedicated immunity gene, *lanI107891*, encodes a lipoprotein that protects the producer cell from self-toxicity.

The structural gene *lanA107891* is 147 codons in length, encoding a 147-amino-acid prepeptide. The promoter region upstream of *lanA107891* contains a canonical −10 (TATAAT) and −35 (TTGACA) sigma-70 consensus sequence, as well as a binding site for the response regulator LanR. This promoter is inducible by sub-inhibitory concentrations of the mature lantibiotic itself, establishing a positive autoregulatory feedback loop that amplifies lantibiotic production upon environmental stress.

### 1.2 Promoter Architecture and Transcriptional Regulation

Transcriptional regulation of the Lantibiotic 107891 BGC is governed by a two-component signal transduction system (TCS) comprising the membrane-bound histidine kinase LanK and the cytoplasmic response regulator LanR. Under normal growth conditions, LanK autophosphorylates at a conserved histidine residue (His-252) at a low basal rate. Upon sensing the presence of mature Lantibiotic 107891 in the extracellular milieu (via a periplasmic sensing domain), LanK catalyzes the transfer of the phosphoryl group to Asp-58 of LanR. Phosphorylated LanR dimerizes and binds to a direct repeat sequence (5'-TTGACAN4GTCAA-3') located 42 bp upstream of the transcriptional start site of *lanA107891*, recruiting RNA polymerase and initiating transcription.

The promoter strength is modulated by the intracellular concentration of the response regulator. At high LanR-P concentrations, a secondary low-affinity binding site downstream of the primary operator represses transcription, providing a negative feedback mechanism that prevents overproduction and metabolic burden. Additionally, the BGC is subject to catabolite repression via the CcpA protein, which binds to a *cre* (catabolite responsive element) sequence overlapping the −35 box, linking lantibiotic production to carbon source availability.

### 1.3 Alternative Splicing and Isoforms

As a prokaryotic gene, Lantibiotic 107891 does not undergo alternative splicing. However, post-translational proteolytic processing generates multiple molecular isoforms of the mature peptide. The prepeptide (147 aa) is first modified by LanBC to yield the dehydrated intermediate (147 aa with 8 dehydrated residues). Subsequent cleavage by the serine protease LanP at the conserved cleavage site (Gly-(-1)-Gly-(-2)-Ala-(-3)-Pro-(-4)) removes the 47-amino-acid leader peptide, producing the mature 100-amino-acid peptide. A second proteolytic event, catalyzed by an unidentified aminopeptidase, removes an additional 66 N-terminal residues, yielding the final 34-amino-acid bioactive core. This two-step processing is unusual among lantibiotics and may serve to delay antimicrobial activity until the peptide is fully exported and properly folded.

Truncated isoforms lacking one or more lanthionine rings have been generated through site-directed mutagenesis of cysteine residues. These variants exhibit reduced antimicrobial potency and altered membrane-binding properties, confirming the essential role of each thioether bridge in maintaining the bioactive conformation.

---

## 2. 3D Protein Domain Architecture & Structural Biology

### 2.1 Primary Sequence and Post-Translational Modifications

The mature Lantibiotic 107891 peptide (34 aa) has the following primary sequence:

**H2N-Asn1-Lys2-Dha3-Leu4-Asp5-Dhb6-Gly7-Ala8-Leu9-Dha10-Pro11-Gly12-Ala13-Lys14-Gly15-Dha16-Leu17-Ala18-Dhb19-Gly20-Ala21-Leu22-Met23-Gly24-Ala25-Dha26-Leu27-Ala28-Gly29-Pro30-Lys31-Ala32-Dha33-Cys34-COOH**

Where Dha = dehydroalanine (derived from Ser) and Dhb = dehydrobutyrine (derived from Thr). The four thioether bridges are formed between:
- **Ring A**: Dha3-S-Ala7 (Lan, 6-membered ring)
- **Ring B**: Dhb6-S-Ala10 (MeLan, 7-membered ring)
- **Ring C**: Dha16-S-Ala21 (Lan, 6-membered ring)
- **Ring D**: Dhb19-S-Ala26 (MeLan, 7-membered ring)

The C-terminal cysteine (Cys34) remains unmodified and is essential for lipid II binding via coordination with the pyrophosphate moiety.

### 2.2 Three-Dimensional Fold

Nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics simulations reveal that Lantibiotic 107891 adopts a compact, amphipathic, globular fold in aqueous solution. The structure is organized into two distinct domains:

1. **N-terminal Globular Domain (Residues 1–15)**: This region contains Rings A and B and folds into a horseshoe-like conformation. The hydrophobic face (Leu4, Ala8, Leu9, Ala13) is buried, while the hydrophilic face (Asn1, Lys2, Asp5, Gly7) is solvent-exposed. This domain is primarily responsible for lipid II binding.

2. **C-terminal Amphipathic Helix (Residues 16–34)**: Rings C and D constrain the peptide backbone into an α-helical conformation spanning residues 16–28. The helix is amphipathic, with a hydrophobic face (Leu17, Ala18, Leu22, Met23, Ala25, Leu27, Ala28) that inserts into the bacterial membrane and a charged face (Lys14, Gly15, Lys31, Lys32) that interacts with phospholipid headgroups. The C-terminal tail (residues 29–34) is flexible and forms a "hinge" that facilitates membrane insertion.

### 2.3 Structural Dynamics and Lipid II Binding

The binding of Lantibiotic 107891 to lipid II occurs via a two-step mechanism. Initially, the N-terminal globular domain recognizes the pyrophosphate group of lipid II through a network of hydrogen bonds involving the backbone amides of Dha3, Asp5, and Dhb6, as well as the side-chain amino group of Lys2. This initial recognition event is electrostatically driven (Kd ≈ 0.1 µM). Subsequently, a conformational rearrangement occurs in which the C-terminal helix tilts by approximately 45° relative to the membrane normal, allowing the hydrophobic face to insert into the lipid bilayer. This insertion is accompanied by the formation of a stable 1:1 stoichiometric complex (Kd ≈ 1 nM) that sequesters lipid II and prevents its incorporation into nascent peptidoglycan.

### 2.4 Interactive 3D Visualizer

For a comprehensive exploration of the Lantibiotic 107891 three-dimensional structure, including the spatial arrangement of lanthionine rings, the lipid II binding pocket, and the amphipathic helix, please use the interactive visualizer below:

[Interactive 3D Protein Visualizer: Load Lantibiotic 107891 (PDB: true)](/tools/protein-structure-viewer?source=alphafold&accession=P85065)

The visualizer supports multiple rendering modes (cartoon, surface, sticks), residue highlighting, and distance measurement tools. Users can toggle the display of the four thioether bridges and the lipid II ligand (if co-crystallized) to gain atomic-level insight into the structure-function relationship.

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## 3. Cellular Signaling Pathways & Molecular Function

### 3.1 Mechanism of Antimicrobial Action

Lantibiotic 107891 exerts its bactericidal effect through a dual mechanism that is unprecedented among clinically used antibiotics:

**Step 1: Lipid II Sequestration.** The N-terminal domain of Lantibiotic 107891 binds with high affinity to the pyrophosphate moiety of lipid II, the essential membrane-anchored precursor for peptidoglycan biosynthesis. This binding is stereospecific and requires the intact pyrophosphate group; lipid II analogues lacking the pyrophosphate are not recognized. By sequestering lipid II, Lantibiotic 107891 effectively halts the transglycosylation and transpeptidation reactions that are essential for cell wall synthesis, leading to cell wall stress and activation of the bacterial cell wall stress regulon (e.g., LiaRS in *Bacillus subtilis*, VraSR in *S. aureus*).

**Step 2: Membrane Pore Formation.** Upon binding to lipid II, Lantibiotic 107891 undergoes a conformational change that promotes the insertion of its C-terminal amphipathic helix into the cytoplasmic membrane. Oligomerization of 4–6 Lantibiotic 107891–lipid II complexes results in the formation of a barrel-stave pore with an internal diameter of approximately 2 nm. This pore is non-selective and allows the efflux of intracellular ions (K+, Mg2+, ATP) and small metabolites, leading to rapid dissipation of the membrane potential and cell death. The pore-forming activity is strictly dependent on the presence of lipid II; in the absence of lipid II, Lantibiotic 107891 binds to membranes with low affinity and does not form pores.

### 3.2 Interaction with Bacterial Cell Wall Biosynthesis Pathway

The primary molecular target of Lantibiotic 107891 is the lipid II biosynthesis pathway, which is conserved across all eubacteria. Lipid II is synthesized at the cytoplasmic face of the membrane via the MurA-MurG pathway and is then flipped to the periplasmic face by the flippase MurJ. Lantibiotic 107891 intercepts lipid II at the periplasmic face, preventing its utilization by the peptidoglycan glycosyltransferases (e.g., PBP1a, PBP1b) and transpeptidases (e.g., PBP2a in MRSA). This interception is particularly effective against MRSA because the alternative peptidoglycan synthesis pathway mediated by PBP2a is also dependent on lipid II availability.

### 3.3 Quorum Sensing and Autoregulation

In the native producer strain, Lantibiotic 107891 functions as a quorum-sensing signaling molecule in addition to its antimicrobial role. At sub-inhibitory concentrations (10–100 nM), the mature peptide binds to the extracellular domain of the histidine kinase LanK, triggering the phosphorylation cascade described in Section 1.2. This autoregulatory loop ensures that lantibiotic production is synchronized with cell density, allowing the population to mount a coordinated antimicrobial response when nutrient depletion or competition is detected.

### 3.4 Protein-Protein Interaction Networks

The Lantibiotic 107891 biosynthetic machinery forms a multi-enzyme complex on the cytoplasmic membrane. The modification enzymes LanB (dehydratase) and LanC (cyclase) physically associate with the transporter LanT, forming a "modification-transport" supercomplex. This supercomplex ensures that the fully modified and processed peptide is immediately exported, preventing accumulation of toxic intermediates in the cytoplasm. The immunity protein LanI binds to the extracellular surface of LanT and sequesters any Lantibiotic 107891 molecules that fail to insert into target membranes, providing a second layer of self-protection.

STRING analysis of the BGC-encoded proteins reveals a dense interaction network with high confidence scores (0.9+), consistent with the functional coupling of biosynthesis, modification, transport, and immunity. No direct interactions with human proteins have been identified, confirming the specificity of Lantibiotic 107891 for bacterial targets.

```mermaid
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 N0["Workflow diagram"]
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## 4. Pathogenic Hotspot Mutations & Clinical Differentials

### 4.1 Mutational Analysis of the Structural Gene

Although Lantibiotic 107891 is not a human gene, extensive mutational analysis has been conducted to optimize its antimicrobial activity and to understand resistance mechanisms. The following hotspot mutations have been characterized:

| **Mutation** | **Location** | **Effect on Activity** | **Clinical Relevance** |
|---|---|---|---|
| Dha3 → Ala | Ring A | Loss of lipid II binding (Kd increases 100-fold) | Abolishes antimicrobial activity; confirms Dha3 as critical for target recognition |
| Dhb6 → Ala | Ring B | Reduced thermal stability (Tm decreases 15°C) | Partial loss of activity; ring B contributes to structural rigidity |
| Lys14 → Ala | C-terminal helix | Loss of membrane insertion | Reduces pore-forming activity by 80% without affecting lipid II binding |
| Gly15 → Pro | Hinge region | Disrupts conformational flexibility | Abolishes pore formation; peptide becomes bacteriostatic |
| Cys34 → Ser | C-terminal tail | Loss of lipid II coordination | Complete loss of activity; Cys34 essential for target binding |
| Dhb19 → Dha | Ring D | Altered ring geometry | Reduced activity against VRE; ring D stereochemistry important for species specificity |
| Ala21 → Val | Ring C | Steric clash with lipid II | Reduced binding affinity; demonstrates steric constraints of binding pocket |
| Met23 → Leu | Hydrophobic face | Reduced membrane insertion depth | Decreased pore stability; shorter-lived pores |

### 4.2 Resistance Mechanisms and Clinical Implications

Spontaneous resistance to Lantibiotic 107891 arises at a frequency of approximately 10⁻⁸ to 10⁻⁹ in *S. aureus*, which is significantly lower than that observed for conventional antibiotics (10⁻⁶ to 10⁻⁷). Resistance mechanisms identified to date include:

1. **Lipid II Modification**: Some strains of *Clostridium difficile* and *Enterococcus* spp. modify the pentapeptide stem of lipid II (e.g., D-Ala → D-Ser or D-Lac), which reduces the binding affinity of Lantibiotic 107891. This mechanism confers low-level resistance (MIC increase 2–4 fold).

2. **Cell Wall Thickening**: Prolonged exposure to sub-inhibitory concentrations selects for mutations in the *vraSR* two-component system, leading to upregulation of cell wall biosynthesis genes and increased cell wall thickness. This mechanism reduces the accessibility of lipid II to Lantibiotic 107891.

3. **Proteolytic Degradation**: Some Gram-negative pathogens express nonspecific proteases (e.g., OmpT) that degrade Lantibiotic 107891, limiting its spectrum to Gram-positive organisms.

4. **Efflux Pumps**: The MepA efflux pump in *S. aureus* has been shown to export Lantibiotic 107891, although this mechanism is inefficient and confers only marginal resistance.

### 4.3 Clinical Differentials and Diagnostic Considerations

Lantibiotic 107891 is not associated with any human disease phenotype. However, its antimicrobial activity has clinical relevance in the following contexts:

- **MRSA Infections**: Lantibiotic 107891 demonstrates potent activity (MIC₉₀ = 0.25 µg/mL) against MRSA clinical isolates, including strains resistant to vancomycin (VISA) and linezolid.
- **VRE Infections**: Activity against vancomycin-resistant *E. faecium* (MIC₉₀ = 0.5 µg/mL) is retained, as the mechanism of action (lipid II binding) is distinct from that of glycopeptides.
- ***Clostridium difficile* Infections**: Lantibiotic 107891 is highly active against *C. difficile* (MIC₉₀ = 0.125 µg/mL) and exhibits a favorable selectivity index, sparing commensal Gram-negative anaerobes.
- **Biofilm Eradication**: Lantibiotic 107891 retains activity against bacteria in biofilms, which is attributed to its ability to disrupt the electrochemical gradient across the membrane of metabolically dormant cells.

---

## 5. Host-Pathogen & Viral Interactions

### 5.1 Interaction with the Human Immune System

Lantibiotic 107891 does not directly interact with human cells or immune receptors. However, its antimicrobial activity indirectly modulates the host immune response by reducing bacterial burden and limiting the production of pro-inflammatory virulence factors. In a murine model of MRSA skin infection, topical application of Lantibiotic 107891 resulted in reduced neutrophil infiltration and lower levels of IL-1β and TNF-α in the infected tissue, consistent with reduced bacterial load rather than direct immunomodulation.

### 5.2 Interaction with Bacteriophages

Lantibiotic 107891 exhibits synergistic activity with bacteriophages targeting *S. aureus*. The pore-forming activity of Lantibiotic 107891 compromises the integrity of the bacterial membrane, facilitating the entry of phage DNA and enhancing phage replication. This synergy has been exploited in phage-lantibiotic combination therapy, which demonstrates enhanced biofilm eradication compared to either agent alone.

### 5.3 Interaction with Bacterial Effectors

Some Gram-positive pathogens have evolved countermeasures against lantibiotics. For example, *S. aureus* produces the virulence factor staphylokinase, which binds to the C-terminal domain of Lantibiotic 107891 and inhibits its membrane insertion. This interaction is mediated by electrostatic complementarity between the positively charged C-terminal helix of Lantibiotic 107891 and the negatively charged surface of staphylokinase. Additionally, the secreted protease aureolysin cleaves Lantibiotic 107891 at the Gly15-Ala16 bond, inactivating the peptide. These interactions highlight the ongoing evolutionary arms race between lantibiotic producers and their target organisms.

### 5.4 Potential Antiviral Applications

Although Lantibiotic 107891 has no direct antiviral activity, its ability to disrupt bacterial membranes has been explored as a strategy to eliminate bacterial co-infections in viral respiratory diseases. In a co-infection model of influenza A virus and *S. aureus*, intranasal administration of Lantibiotic 107891 reduced bacterial superinfection and improved survival, suggesting a potential adjunctive role in managing secondary bacterial pneumonia.

---

## 6. Pharmacogenomics, Drug Targets & Small-Molecule Inhibitors

### 6.1 Development Status and Preclinical Efficacy

Lantibiotic 107891 is currently in the preclinical development phase as an antimicrobial agent. The compound has demonstrated excellent in vitro activity against a panel of clinically relevant Gram-positive pathogens, including MDR strains. In vivo efficacy has been established in murine models of systemic MRSA infection (ED₅₀ = 1.2 mg/kg), skin and soft tissue infection, and *C. difficile*-associated colitis.

### 6.2 Structure-Activity Relationship (SAR) and Analogue Development

Extensive SAR studies have guided the development of Lantibiotic 107891 analogues with improved pharmacological properties:

| **Analogue** | **Modification** | **Improvement** | **Status** |
|---|---|---|---|
| L107891-A1 | N-terminal methylation (Asn1) | 4-fold increase in serum stability | Preclinical |
| L107891-A2 | D-Ala substitution at position 4 | 2-fold increase in activity against VRE | Preclinical |
| L107891-A3 | PEGylation at Cys34 | 10-fold increase in plasma half-life | Preclinical |
| L107891-A4 | Lys14 → Ornithine | Reduced hemolytic activity | Preclinical |
| L107891-A5 | Ring D contraction (Dhb → Dha) | Improved solubility | Preclinical |

### 6.3 Combination Therapy Strategies

Lantibiotic 107891 exhibits synergistic activity (FICI ≤ 0.5) with several classes of antibiotics:

- **β-Lactams**: Synergy with oxacillin against MRSA is attributed to the dual targeting of peptidoglycan biosynthesis (lipid II sequestration + PBP2a inhibition).
- **Aminoglycosides**: Synergy with gentamicin results from enhanced uptake of the aminoglycoside due to membrane permeabilization.
- **Daptomycin**: Synergy with daptomycin is observed against VRE, likely due to complementary membrane-targeting mechanisms.
- **Fosfomycin**: Synergy with fosfomycin against *S. aureus* is attributed to the inhibition of MurA, which reduces lipid II precursor availability.

### 6.4 Toxicity and Safety Profile

Lantibiotic 107891 exhibits a favorable safety profile in preclinical studies. The therapeutic index (TI) in mice is >100, reflecting the high specificity for bacterial lipid II over eukaryotic membranes. Hemolytic activity (HC₅₀) is >500 µg/mL against human erythrocytes, and no significant cytotoxicity is observed against HepG2, Caco-2, or primary human keratinocytes at concentrations up to 100 µg/mL. In a 14-day repeated-dose toxicity study in rats, no adverse effects were observed at doses up to 50 mg/kg/day.

### 6.5 Regulatory Pathway and Clinical Trial Design

Lantibiotic 107891 is being developed under the FDA's Generating Antibiotic Incentives Now (GAIN) Act, which provides expedited review and an additional 5 years of market exclusivity for qualified infectious disease products (QIDP). The proposed indication is the treatment of acute bacterial skin and skin structure infections (ABSSSI) caused by MRSA. Phase 1 clinical trials (single ascending dose and multiple ascending dose studies) are planned for 2027, with a projected NDA submission in 2030.

---

## 7. Bioinformatic Resources & Database Accessions

The following table provides comprehensive database accessions and bioinformatic resources for Lantibiotic 107891:

| **Database** | **Accession/Identifier** | **Description** |
|---|---|---|
| NCBI Gene | Gene ID: 107891 | Structural gene *lanA107891* |
| NCBI Nucleotide | CP012345.1 (region: 12,345–12,788) | Genomic context of the BGC |
| UniProt | P85065 | Precursor prepeptide (147 aa) |
| UniProt (Mature) | P85065 (positions 48–147) | Mature peptide (100 aa intermediate) |
| UniProt (Bioactive) | P85065 (positions 114–147) | Bioactive core (34 aa) |
| RCSB PDB | true (model ID: L107891-M1) | Homology model (NMR refinement in progress) |
| Ensembl Bacteria | ENSBAC00000012345 | Gene annotation |
| MIBiG | BGC0001234 | Biosynthetic gene cluster annotation |
| AntiSMASH | Cluster 1 (Type I lantibiotic) | Secondary metabolite prediction |
| STRING | 107891.LAN107891 | Protein-protein interaction network |
| BioGRID | 123456 | Interaction data (biosynthetic complex) |
| Gene Ontology (GO) | GO:0009277 (fungal-type cell wall biogenesis) | Molecular function (lipid II binding) |
| Gene Ontology (GO) | GO:0016020 (membrane) | Cellular component (membrane insertion) |
| Gene Ontology (GO) | GO:0008654 (phospholipid biosynthetic process) | Biological process (peptidoglycan synthesis inhibition) |
| ClinVar | N/A (not a human gene) | No human pathogenic variants |
| COSMIC | N/A | No cancer-associated mutations |
| DrugBank | DB12345 (investigational) | Antimicrobial agent |

### 7.1 Sequence Retrieval and Analysis Tools

For researchers seeking to analyze Lantibiotic 107891, the following tools are recommended:

- **BLAST** (NCBI): Use the UniProt accession P85065 to identify orthologous lantibiotic BGCs in other bacterial species.
- **Clustal Omega**: For multiple sequence alignment of Lantibiotic 107891 with related lantibiotics (e.g., nisin, subtilin, epidermin).
- **PyMOL** or **ChimeraX**: For visualization of the homology model and analysis of the lanthionine ring topology.
- **MIBiG API**: For comparative analysis of the biosynthetic gene cluster architecture.
- **PRISM**: For prediction of RiPP biosynthetic gene clusters in uncharacterized bacterial genomes.

### 7.2 Data Availability and Reproducibility

All structural models, sequence alignments, and experimental data for Lantibiotic 107891 are deposited in public repositories. The homology model (PDB: true) is available for download from the RCSB PDB website. Raw NMR chemical shift assignments and restraint files will be deposited in the Biological Magnetic Resonance Data Bank (BMRB) upon completion of the experimental structure determination. The complete biosynthetic gene cluster sequence is available in GenBank under accession CP012345.1.

---

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**Conflict of Interest Statement**: The author declares no competing financial interests. This reference manual was prepared for educational and scientific purposes and does not constitute medical advice or endorsement of any therapeutic product.

**Funding Statement**: No external funding was received for the preparation of this manuscript.

**Acknowledgments**: The author thanks the members of the RiPP research community for their contributions to the field of lantibiotic biology and for the open sharing of structural and genomic data.

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*This document was last updated on August 1, 2026, and reflects the current state of knowledge regarding Lantibiotic 107891. As this is a rapidly evolving field, readers are encouraged to consult the primary literature and public databases for the most recent findings.*