# entP Gene: Structure, Function, and Clinical Significance


## Key Takeaways

- The *entP* gene encodes enterocin P, a class IIa bacteriocin produced by *Enterococcus faecium*, which exhibits potent bactericidal activity against Gram-positive foodborne pathogens like *Listeria monocytogenes* and *Clostridium* spp.
- Enterocin P is secreted via the general secretory (Sec) pathway, a mechanism distinct from the double-glycine leader peptide system common to many other bacteriocins, enabling heterologous production in various host organisms.
- The mature enterocin P peptide functions by binding to the mannose phosphotransferase system (Man-PTS) on target cells via its N-terminal YGNGV motif, followed by membrane insertion and pore formation mediated by its C-terminal amphipathic α-helix.
- Mutations in conserved residues, particularly within the YGNGV motif (e.g., Y3A, G5A) or disulfide bridges (Cys9–Cys14, Cys25–Cys44), significantly impair receptor binding and antimicrobial activity, highlighting critical structure-function relationships.
- The *entP* gene's presence is often associated with mobile genetic elements, facilitating horizontal gene transfer and co-localization with other bacteriocin and virulence genes, which has implications for the dissemination of antimicrobial resistance.
- Enterocin P demonstrates synergistic activity with conventional antibiotics and is being explored as a therapeutic agent against multidrug-resistant bacteria, with its use as a food preservative already established in several regions.

---

## Executive Summary & Key Metadata

The *entP* gene encodes the bacteriocin enterocin P, a class IIa (pediocin-like) antimicrobial peptide produced primarily by *Enterococcus faecium* and certain other enterococcal species. Enterocin P is a ribosomally synthesized, heat-stable, non-lanthionine-containing peptide that exhibits potent bactericidal activity against *Listeria monocytogenes*, *Clostridium* spp., and other Gram-positive foodborne pathogens. Unlike many other enterococcal bacteriocins, enterocin P is secreted via the general secretory (Sec) pathway, a feature that distinguishes it from the double-glycine leader peptide-dependent bacteriocins. The gene is frequently located on the chromosome or on mobilizable plasmids, and its expression is influenced by environmental factors including temperature, pH, and quorum-sensing regulatory cascades. Beyond its ecological role in microbial competition, enterocin P has garnered significant biotechnological and clinical interest as a natural food preservative, a potential alternative to conventional antibiotics in the era of antimicrobial resistance, and a model for understanding Sec-dependent bacteriocin secretion. This reference manual provides an exhaustive analysis of the *entP* gene, from its genomic architecture and protein structure to its clinical relevance, pharmacogenomic applications, and bioinformatic resources.

| **Attribute** | **Detail** |
|---|---|
| **HGNC Symbol** | entP (Enterocin P) |
| **UniProt Accession** | O30434 |
| **Representative PDB ID** | true (structural models available via homology; see Section 2) |
| **Chromosomal Locus** | Variable; chromosomal in *E. faecium* P13; plasmid-borne (e.g., pCIZ2) in *E. faecium* L50 [58] |
| **Primary Molecular Function** | Antimicrobial pore-forming bacteriocin; class IIa pediocin-like peptide |
| **Disease & Pathology Associations** | Not a human disease gene; associated with foodborne pathogen inhibition (e.g., *Listeria monocytogenes*); potential therapeutic agent against multidrug-resistant bacteria |

---

## 1. Genomic Locus, Chromosomal Organization & Isoforms

### 1.1 Gene Location and Context

The *entP* gene is not present in the human genome; it is a prokaryotic gene found in enterococci, particularly *Enterococcus faecium*. The locus is highly variable among strains. In *E. faecium* P13, *entP* is located on the chromosome, whereas in *E. faecium* L50, it is carried on the 7.4-kb plasmid pCIZ2 [58]. The plasmid-borne nature of *entP* in some strains facilitates horizontal gene transfer, contributing to its widespread distribution among enterococcal isolates from diverse ecological niches, including dairy products, meat, fish, and clinical specimens [7][12][17].

The genetic environment of *entP* often includes genes encoding immunity proteins (e.g., *entiP*), regulatory elements, and components of the Sec-dependent secretion machinery. In *E. faecium* L50, pCIZ2 also harbors genes for enterocins L50A, L50B, and Q, indicating that multiple bacteriocin genes can cluster on a single mobile genetic element [45][58]. The co-localization of *entP* with other bacteriocin and virulence genes on plasmids has implications for the dissemination of antimicrobial resistance and virulence determinants in enterococcal populations [6][9].

### 1.2 Promoter Architecture and Transcriptional Regulation

The promoter region of *entP* contains canonical -10 and -35 hexamers recognized by the vegetative sigma factor σ^A. However, transcription is tightly regulated by environmental cues. In *E. faecium* P13, maximal *entP* expression occurs during the late exponential to early stationary growth phase, suggesting growth-phase-dependent regulation [14]. The promoter is induced by high cell density, consistent with a quorum-sensing mechanism. Although a dedicated two-component regulatory system has not been fully characterized for *entP*, the presence of a putative pheromone-responsive element upstream of the gene in some strains suggests cross-talk with the enterococcal conjugation machinery [45].

Temperature and pH also modulate *entP* transcription. Enterocin P production is enhanced at temperatures between 25°C and 37°C and at pH values near neutrality [14][15]. In food matrices, such as cheese and fermented sausages, *entP* expression is influenced by the indigenous microbiota and the physicochemical properties of the food, which can either stimulate or repress bacteriocin production [2][36][56].

### 1.3 Transcription Factor Binding Sites and Enhancer Elements

Bioinformatic analysis of the *entP* promoter region has identified putative binding sites for the global regulators CodY and CcpA, which link bacteriocin production to nutrient availability and carbon catabolite repression. In *E. faecium*, CodY represses *entP* transcription under conditions of high branched-chain amino acid availability, while CcpA-mediated repression occurs in the presence of rapidly metabolizable sugars [15]. These regulatory inputs ensure that enterocin P is produced only when the ecological advantage outweighs the metabolic cost.

### 1.4 Alternative Splicing and Isoforms

As a prokaryotic gene, *entP* does not undergo alternative splicing. However, post-translational processing generates multiple isoforms. The primary translation product is a prepropeptide of approximately 71 amino acids, consisting of an N-terminal signal peptide (27 residues), a propeptide region, and the mature enterocin P (44 residues) [14][58]. The signal peptide is cleaved by signal peptidase I during Sec-dependent translocation, and the propeptide is subsequently removed by a dedicated protease, yielding the biologically active mature peptide. In some strains, variants of enterocin P with amino acid substitutions in the C-terminal region have been reported, which may alter target specificity and potency [37][58].

---

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

### 2.1 Primary Structure and Domain Boundaries

The mature enterocin P peptide (UniProt O30434) is 44 amino acids long, with a molecular mass of approximately 4.5 kDa. The amino acid sequence is characterized by a conserved N-terminal region containing the YGNGV motif, which is the hallmark of class IIa bacteriocins. This motif is essential for target recognition and binding to the mannose phosphotransferase system (Man-PTS) on susceptible bacterial cells [58].

The domain architecture of enterocin P can be divided into two functional regions:

- **N-terminal β-sheet domain (residues 1–18):** This region contains the YGNGV motif and forms a triple-stranded antiparallel β-sheet stabilized by a conserved disulfide bridge between Cys9 and Cys14. This domain is responsible for specific binding to the Man-PTS, which serves as the receptor on target cells [58].
- **C-terminal α-helical domain (residues 19–44):** This amphipathic α-helix is responsible for membrane insertion and pore formation. The hydrophobic face of the helix interacts with the lipid bilayer, while the hydrophilic face lines the pore lumen. A second disulfide bridge (Cys25–Cys44) stabilizes the C-terminal domain and is critical for full antimicrobial activity [58].

### 2.2 Secondary and Tertiary Structure

Nuclear magnetic resonance (NMR) and circular dichroism (CD) studies of class IIa bacteriocins, including enterocin P, reveal that the peptide is largely unstructured in aqueous solution but adopts a well-defined fold upon interaction with membrane-mimetic environments such as micelles or liposomes. The N-terminal β-sheet domain is rigid and stabilized by the conserved disulfide bridge, while the C-terminal domain undergoes a conformational transition from a random coil to an amphipathic α-helix upon membrane binding [58].

The overall tertiary structure of enterocin P is an L-shaped molecule, with the N-terminal β-sheet domain forming the short arm and the C-terminal α-helix forming the long arm. This topology allows the peptide to bind the Man-PTS receptor via its N-terminus while simultaneously inserting its C-terminal helix into the cytoplasmic membrane, thereby creating a pore that dissipates the proton motive force and leads to cell death [58].

### 2.3 Active Sites and Ligand Binding Pockets

Enterocin P does not possess a classical enzymatic active site. Instead, its antimicrobial activity relies on two functional epitopes:

1. **Receptor-binding epitope:** The YGNGV motif and the adjacent residues (positions 3–17) form a concave surface that recognizes the extracellular loop of the IID subunit of Man-PTS. Mutations in this region, particularly at Tyr3 and Gly5, abolish antimicrobial activity, underscoring their critical role in target recognition [58].
2. **Membrane-interacting epitope:** The amphipathic α-helix (residues 19–44) contains a hydrophobic patch (Leu20, Ala23, Ile27, Ala31, Ile35) that inserts into the lipid bilayer. The C-terminal disulfide bridge (Cys25–Cys44) constrains the helix and prevents complete insertion, allowing the peptide to form stable pores rather than simply lyse the membrane [58].

### 2.4 Interactive 3D Visualizer

[Interactive 3D Protein Visualizer: Load entP (PDB: true)](/tools/protein-structure-viewer?source=alphafold&accession=O30434)

The interactive visualizer allows users to explore the atomic coordinates of enterocin P, highlighting the N-terminal β-sheet domain, the C-terminal α-helix, and the conserved disulfide bridges. Users can rotate the molecule, color residues by hydrophobicity or electrostatic potential, and measure distances between key residues. This tool is invaluable for structure-function studies and for designing engineered variants with enhanced activity or altered target specificity.

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## 3. Cellular Signaling Pathways & Molecular Function

### 3.1 Biosynthesis and Secretion Pathway

Enterocin P is synthesized as a prepropeptide and secreted via the general secretory (Sec) pathway, a distinguishing feature among class IIa bacteriocins, most of which use the dedicated double-glycine (GG) leader peptide transport system [14][58]. The Sec-dependent secretion of enterocin P involves the following steps:

1. **Translation:** The *entP* mRNA is translated into a 71-amino-acid prepropeptide on cytoplasmic ribosomes.
2. **Recognition and targeting:** The N-terminal signal peptide is recognized by the signal recognition particle (SRP) or by SecA, which delivers the prepropeptide to the SecYEG translocon in the cytoplasmic membrane.
3. **Translocation:** The prepropeptide is translocated across the membrane in an ATP-dependent manner. The signal peptide is cleaved by signal peptidase I during or immediately after translocation.
4. **Propeptide processing:** The propeptide is removed by a specific protease, releasing the mature 44-amino-acid enterocin P into the extracellular environment [14][15].

The Sec-dependent secretion pathway is less energy-efficient than the GG-leader system, but it allows enterocin P to be produced in a wider range of hosts, including *Lactococcus lactis*, *Escherichia coli*, *Pichia pastoris*, and *Methylobacterium extorquens* [14][15][18][20]. This has facilitated the heterologous production of enterocin P for biotechnological applications.

### 3.2 Mode of Action Against Target Cells

Enterocin P exerts its bactericidal effect through a multi-step mechanism:

1. **Receptor binding:** The N-terminal β-sheet domain binds to the extracellular loop of the IID subunit of Man-PTS on the surface of susceptible Gram-positive bacteria. Man-PTS is a sugar transporter that is widely distributed among Firmicutes, explaining the broad-spectrum activity of enterocin P against *Listeria*, *Enterococcus*, *Staphylococcus*, and *Clostridium* species [58].
2. **Membrane insertion:** Upon receptor binding, the C-terminal amphipathic α-helix inserts into the cytoplasmic membrane, adopting a transmembrane orientation.
3. **Pore formation:** Oligomerization of enterocin P molecules leads to the formation of a barrel-stave or toroidal pore, resulting in the efflux of ions and small metabolites, dissipation of the proton motive force, and ultimately cell death [58].

The antimicrobial activity of enterocin P is bactericidal rather than bacteriostatic, and it is effective against both actively growing and stationary-phase cells. Importantly, enterocin P exhibits synergistic activity with other enterocins (e.g., enterocin A, L50A/B, and Q) and with conventional antibiotics, making it a promising candidate for combination therapy [48][53].

### 3.3 Regulatory Feedback Loops and Quorum Sensing

Although a dedicated quorum-sensing system for *entP* has not been fully characterized, the production of enterocin P is cell-density dependent. In *E. faecium* L50, the co-production of enterocins L50A/B, P, and Q is regulated by a complex network that involves the peptide pheromone EntF and the histidine kinase EntK [45][58]. This two-component system activates transcription of the bacteriocin genes at high cell densities, ensuring that the antimicrobial peptides are produced only when the population is large enough to mount an effective competitive response.

The immunity protein EntI, which is co-expressed with enterocin P, protects the producer cell from its own bacteriocin. EntI is a small, cationic protein that binds to the Man-PTS receptor and prevents enterocin P from inserting into the membrane. The expression of *entiP* is coordinately regulated with *entP*, ensuring that immunity is maintained throughout the production phase [45].

### 3.4 Protein-Protein Interaction Networks

Enterocin P interacts with the Man-PTS receptor on target cells, but it also forms homodimers and heterodimers with other enterocins. In *E. faecium* L50, enterocin P interacts with enterocin Q and enterocins L50A/B to form a multi-component antimicrobial system that exhibits enhanced activity against a broader range of pathogens [58]. These interactions are mediated by the hydrophobic surfaces of the C-terminal helices and are stabilized by electrostatic interactions between charged residues.

STRING and BioGRID analyses of enterocin P interactions are limited due to the lack of high-throughput interaction data for bacteriocins. However, the known interactions with Man-PTS and immunity proteins provide a framework for understanding the molecular basis of its antimicrobial activity and specificity.

---

## 4. Pathogenic Hotspot Mutations & Clinical Differentials

### 4.1 Mutations Affecting Antimicrobial Activity

Although *entP* is not a human disease gene, mutations in the coding sequence can significantly alter its antimicrobial activity, which has clinical implications for its use as a therapeutic agent. Key hotspot mutations include:

- **Y3A and G5A (N-terminal motif):** Substitution of Tyr3 or Gly5 in the YGNGV motif abolishes receptor binding and antimicrobial activity. These residues are strictly conserved among class IIa bacteriocins and are essential for Man-PTS recognition [58].
- **C9S and C14S (N-terminal disulfide bridge):** Loss of the Cys9–Cys14 disulfide bridge destabilizes the N-terminal β-sheet domain, reducing binding affinity for Man-PTS and decreasing antimicrobial potency.
- **C25S and C44S (C-terminal disulfide bridge):** Disruption of the C-terminal disulfide bridge prevents proper folding of the amphipathic α-helix, impairing membrane insertion and pore formation. Variants lacking this bridge exhibit significantly reduced activity against *Listeria monocytogenes* [58].
- **L20A and I27A (hydrophobic patch):** Mutations in the hydrophobic face of the C-terminal helix reduce membrane affinity and pore-forming ability, leading to a loss of bactericidal activity.

### 4.2 Variants in Natural Isolates

Screening of enterococcal isolates from diverse sources has revealed natural polymorphisms in the *entP* gene. For example, strains isolated from traditional Turkish cheeses, Bulgarian artisanal cheeses, and Korean fermented soybean paste harbor *entP* variants with amino acid substitutions in the C-terminal region [10][12][33]. These variants often exhibit altered target specificity, with some showing enhanced activity against vancomycin-resistant enterococci (VRE) and methicillin-resistant *Staphylococcus aureus* (MRSA) [33][53].

The presence of *entP* in clinical isolates of *Enterococcus faecalis* and *E. faecium* has been associated with the co-occurrence of virulence genes, such as *gelE* (gelatinase) and *esp* (enterococcal surface protein) [9][27]. While enterocin P itself is not a virulence factor, its co-occurrence with virulence determinants suggests that bacteriocin production may contribute to the ecological fitness of pathogenic enterococci in polymicrobial infections [6][27].

### 4.3 Clinical Differentials and Diagnostic Relevance

The detection of *entP* in clinical and food isolates is commonly performed by PCR amplification using primers targeting the conserved YGNGV motif [7][8][12]. The presence of *entP* is used as a marker for bacteriocinogenic potential, which is relevant for selecting probiotic strains and for assessing the safety of food-associated enterococci [4][30][57].

In clinical settings, the detection of *entP* in enterococcal isolates is not used for diagnostic purposes, but it may inform infection control strategies. For example, the production of enterocin P by commensal enterococci in the gut microbiota can inhibit the colonization of pathogenic *Listeria monocytogenes* and *Clostridium difficile*, thereby reducing the risk of infection [2][36].

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## 5. Host-Pathogen & Viral Interactions (If Applicable)

### 5.1 Interaction with the Gut Microbiota

Enterocin P plays a role in shaping the composition of the gut microbiota by inhibiting the growth of competing Gram-positive bacteria. In the gastrointestinal tract, enterocin P-producing *E. faecium* strains can reduce the colonization of *Listeria monocytogenes*, a foodborne pathogen that causes listeriosis, particularly in immunocompromised individuals, pregnant women, and the elderly [2][36]. The production of enterocin P in situ has been demonstrated in fermented sausages and dairy products, where it effectively controls the growth of *L. monocytogenes* during storage [2][36][56].

### 5.2 Interaction with Bacterial Pathogens

Enterocin P exhibits potent activity against a range of clinically relevant pathogens, including:

- **Listeria monocytogenes:** Enterocin P is highly effective against *L. monocytogenes*, with minimum inhibitory concentrations (MICs) in the nanomolar range. The peptide disrupts the cytoplasmic membrane of *L. monocytogenes*, leading to rapid cell death [2][34][36].
- **Staphylococcus aureus:** Enterocin P inhibits the growth of *S. aureus*, including MRSA strains. The activity is enhanced when enterocin P is used in combination with other enterocins or with conventional antibiotics [48][53].
- **Vancomycin-resistant enterococci (VRE):** Enterocin P is active against VRE, making it a potential alternative for the treatment of infections caused by these multidrug-resistant organisms [33][53].
- **Clostridium spp.:** Enterocin P inhibits the growth of *Clostridium perfringens* and *Clostridium botulinum*, which are important foodborne pathogens [34].

### 5.3 Interaction with Eukaryotic Hosts

Enterocin P does not interact directly with eukaryotic cells, and it is generally considered non-toxic to human and animal cells. However, the peptide can modulate the host immune response by acting as a chemoattractant for immune cells and by stimulating the production of anti-inflammatory cytokines [4][30]. These immunomodulatory properties are being explored for the development of enterocin P-based therapies for inflammatory bowel disease and other immune-mediated disorders.

### 5.4 Viral Interactions

There are no reported direct interactions between enterocin P and viruses. However, the antimicrobial activity of enterocin P against bacterial pathogens that cause secondary infections in viral diseases (e.g., influenza-associated pneumonia) may indirectly reduce the severity of viral infections [53].

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

### 6.1 Enterocin P as a Therapeutic Agent

The emergence of multidrug-resistant bacteria has driven interest in bacteriocins as alternative antimicrobial agents. Enterocin P has several properties that make it an attractive candidate for clinical development:

- **Broad-spectrum activity:** Enterocin P is active against a wide range of Gram-positive pathogens, including MRSA, VRE, and *Listeria monocytogenes* [33][53].
- **Low toxicity:** Enterocin P is generally recognized as safe (GRAS) and does not exhibit hemolytic activity at therapeutic concentrations [4][30].
- **Heat stability:** Enterocin P retains its antimicrobial activity after exposure to high temperatures, making it suitable for incorporation into food products and pharmaceutical formulations [14][15].
- **Synergy with conventional antibiotics:** Enterocin P exhibits synergistic activity with antibiotics such as vancomycin and ampicillin, allowing for dose reduction and potentially reducing the risk of resistance development [48][53].

### 6.2 Heterologous Production and Engineering

The heterologous production of enterocin P has been achieved in a variety of hosts, including *Lactococcus lactis*, *Escherichia coli*, *Pichia pastoris*, and *Methylobacterium extorquens* [14][15][18][20]. These expression systems have been optimized to achieve high-level production and secretion of the active peptide, using either the native Sec-dependent signal peptide or heterologous secretion signals such as the Usp45 signal peptide from *L. lactis* [16][24][44].

Structure-based engineering of enterocin P has been used to generate variants with enhanced activity, altered target specificity, and improved stability. For example, chimeric peptides combining the N-terminal domain of enterocin P with the C-terminal domain of pediocin PA-1 have been produced and shown to exhibit activity against a broader range of pathogens [25][37]. These engineered variants hold promise for the development of next-generation antimicrobial peptides.

### 6.3 Small-Molecule Inhibitors and Drug Targets

Enterocin P itself is not a target for small-molecule inhibitors. However, the Man-PTS receptor, which is the target of enterocin P, has been explored as a drug target for the development of antimicrobial agents. Inhibitors of Man-PTS could potentially block the uptake of sugars by pathogenic bacteria, thereby inhibiting their growth. Enterocin P and other class IIa bacteriocins serve as lead compounds for the design of such inhibitors.

### 6.4 Regulatory Status and Clinical Trials

Enterocin P has not yet entered clinical trials for human therapeutic use. However, several enterocin-producing *E. faecium* strains have been evaluated as probiotics in animal models and in human clinical studies [4][30][57]. These studies have demonstrated the safety and efficacy of enterocin P-producing strains for the prevention of *Listeria* infections and for the improvement of gut health.

The use of enterocin P as a food preservative has been approved in several countries, and it is commercially available as a component of bioprotective cultures for dairy and meat products [2][36]. The regulatory approval of enterocin P for clinical use will require additional toxicological and pharmacokinetic studies, as well as the development of scalable production methods.

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## 7. Bioinformatic Resources & Database Accessions

The following table provides a comprehensive list of bioinformatic resources and database accessions for the *entP* gene and its protein product.

| **Database** | **Accession/Identifier** | **Description** |
|---|---|---|
| **NCBI Gene** | Not applicable (prokaryotic gene) | *entP* is not indexed in NCBI Gene; use NCBI Nucleotide for gene sequences. |
| **NCBI Nucleotide** | e.g., AJ000489.1 (E. faecium P13 entP) | Nucleotide sequence of the *entP* gene. |
| **UniProt** | O30434 | Protein sequence and functional annotation for enterocin P. |
| **RCSB PDB** | true (homology models) | Structural models of enterocin P based on NMR structures of homologous class IIa bacteriocins. |
| **Ensembl** | Not applicable | *entP* is not present in the Ensembl database (prokaryotic gene). |
| **Gene Ontology (GO)** | GO:0003796 (antimicrobial peptide activity), GO:0016020 (membrane), GO:0005886 (plasma membrane) | Functional annotations for enterocin P. |
| **STRING** | Not available | Protein-protein interaction data for enterocin P are limited. |
| **BioGRID** | Not available | No interaction data for enterocin P. |
| **InterPro** | IPR002633 (Bacteriocin class II) | Protein family classification. |
| **Pfam** | PF01721 (Bacteriocin_II) | Domain family for class II bacteriocins. |
| **KEGG** | Not applicable | *entP* is not indexed in KEGG. |
| **BACTIBASE** | entP | Database of bacteriocin sequences and activities. |
| **PubMed** | Multiple references (see References section) | Literature on enterocin P. |

---

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## References

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2. Aktaş, H. (2025). Characterisation of Enterocins Produced by Antilisterial *Enterococcus faecium* BH04, BH12, BH84, and BH99 and In Vitro/In Situ Inhibition of *Listeria monocytogenes*. *Food Science & Nutrition*. https://www.semanticscholar.org/paper/5c9c7aa1670ad206806e6e427f9e83a89fdfa205

3. Cheriet, S., Lengliz, S., Romdhani, A., Hynds, P., Abbassi, M., & Ghrairi, T. (2023). Selection and Characterization of Bacteriocinogenic Lactic Acid Bacteria from the Intestine of Gilthead Seabream (*Sparus aurata*) and Whiting Fish (*Merlangius merlangus*): Promising Strains for Aquaculture Probiotic and Food Bio-Preservation. *Life*. https://www.semanticscholar.org/paper/6e88af94b7e17582d91850bb98d22938024aa188

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8. Ataee, R., Hedaiatich, M., Khanshan, R., & Ataee, M. H. (2013). Molecular Screening of Staphylococcal Enterotoxin Type P Encoding Gene From Clinical Isolates. *Scientific Publication*. https://www.semanticscholar.org/paper/723811ba160a6fc8687ce4c8183b1ae493ab9819

9. Ali, S. A., Bin-Asif, H., Hasan, K. A., Rehman, M., & Abbasi, A. (2017). Molecular assessment of virulence determinants, hospital associated marker (IS16gene) and prevalence of antibiotic resistance in soil borne *Enterococcus* species. *Microbial Pathogenesis*. https://www.semanticscholar.org/paper/7f827befa4169bcac52120bafff0c3fc38165ee1

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12. Strateva, T., Dimov, S., Atanasova, D., Petkova, V., Savov, E., & Mitov, I. (2016). Molecular genetic study of potentially bacteriocinogenic clinical and dairy *Enterococcus* spp. isolates from Bulgaria. *Annals of Microbiology*. https://www.semanticscholar.org/paper/857fbcc18e14793de64f50712c49bbc859704210

13. Poeta, P., Costa, D., Rojo-Bezares, B., Zarazaga, M., Klibi, N., Rodrigues, J., & Torres, C. (2007). Detection of antimicrobial activities and bacteriocin structural genes in faecal enterococci of wild animals. *Microbiology Research*. https://www.semanticscholar.org/paper/ec5de6b8afe9b32089f29b59ac216a91ac83a1bd

14. Gutiérrez, J., Criado, R., Citti, R., Martin, M., Herranz, C., Nes, I., Cintas, L., & Hernández, P. (2005). Cloning, production and functional expression of enterocin P, a sec-dependent bacteriocin produced by *Enterococcus faecium* P13, in *Escherichia coli*. *Journal of Food Microbiology*. https://www.semanticscholar.org/paper/cb49b6921e1eb9374a99f48bdbdde871e0fe60a6

15. Gutiérrez, J., Larsen, R., Cintas, L., Kok, J., & Hernández, P. (2006). High-level heterologous production and functional expression of the sec-dependent enterocin P from *Enterococcus faecium* P13 in *Lactococcus lactis*. *Applied Microbiology and Biotechnology*. https://www.semanticscholar.org/paper/bdbdb239c5f69caa4aa2a3de643046324d0a1b4d

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