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| Description | GMPRGA (CAS: 2059978-58-2) is the 6-residue arbitrium communication signal AimP secreted by the Bacillus subtilis SPbeta phage, sequence Gly-Met-Pro-Arg-Gly-Ala. Molecular formula C23H41N9O7S, MW 587.69 Da. GMPRGA is specifically recognized by the cytosolic AimR TPR-domain transcription factor, inhibiting AimR DNA binding and switching off aimX (a negative lysogeny regulator) to drive the phage from lysis to lysogeny late in infection. GMPRGA is a homolog of the phi3T peptide SAIRGA within the arbitrium family. It is a tool for phage arbitrium communication, lysogeny-lysis population decisions, AimR-AimP receptor-ligand interactions, and cross-kingdom microbe-phage signaling. |
| Structure type | Linear 6-mer (B. subtilis SPbeta phage arbitrium AimP hexapeptide) |
| Solubility | Readily soluble in water, dilute acetic acid |
| Storage | Powder -20C, dry, protected from light |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| GMPRGA (free base) | GMPRGA free base; Gly-Met-Pro-Arg-Gly-Ala; Spbeta phage AimR-inducing hexapeptide; lysogeny-lysis decision hexapeptide | hexapeptide, phage peptide, Spbeta, spAimR ligand, lysogeny-lysis switch, PPI probe, free base, Met oxidation-sensitive, short active peptide, synthetic biology switch | Linear 6-aa peptide, sequence Gly1-Met2-Pro3-Arg4-Gly5-Ala6 (Gly-Met-Pro-Arg-Gly-Ala), derived from the Spbeta-like phage AimP/AimX/AimR lysogeny regulatory system; free N-terminus +1, Arg side chain guanidinium +1, free C-terminus -1, no acidic residues, net charge ~+1; contains one Met (oxidation-sensitive), one Pro (conformational restriction), one Arg; 50% hydrophobic residues (Met, Pro, Ala); no Cys, Trp, His, no disulfide; short, flexible, hydrophilic, can diffuse into bacterial cytosol to bind spAimR | C23H41N9O7S | 587.29 | 587.70 | Free base; free N-terminal amine and free C-terminal carboxyl, no counterion (distinct from the TFA salt form) | 6 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-GMPRGA-01 | White powder | -20°C, desiccated, sealed, light-protected; contains Met which is prone to oxidation; flush with argon/nitrogen before sealing; avoid repeated freeze-thaw | 2-8°C, desiccated and light-protected, stable for 1-2 weeks | Short, net +1, largely hydrophilic peptide; readily soluble in water or aqueous buffers (PBS, Tris-HCl). The Met residue is easily oxidized to Met sulfoxide in solution, so prepare fresh and aliquot for -20°C storage; no DMSO needed; although there is no Trp, Met-containing peptides are best kept in brown tubes | Met is relatively stable; for long-term storage keep dry at -20°C under inert gas; short peptides are hygroscopic, seal tightly |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-GMPRGA-01 | A Spbeta-phage-derived hexapeptide free base (Gly-Met-Pro-Arg-Gly-Ala) that binds spAimR in the bacterial cytosol to trigger the phage lysogeny-lysis decision; net charge +1, Met oxidation-sensitive. | GMPRGA is a six-residue signaling peptide derived from the lysogeny-lysis regulatory system of Bacillus subtilis Spbeta-like phages. In the Spbeta immune circuit, the phage proteins AimP/AimX sense host DNA damage (the SOS response) and proteolytically release a small peptide signal whose core active motif is GMPRGA. This hexapeptide diffuses in the bacterial cytosol and specifically binds the phage-encoded cI-like repressor spAimR (AimR immune protein), allosterically activating its cI-like repressor domain, shutting off phage lytic genes and maintaining lysogeny. Structural and functional work by Dou et al. (Nature Microbiology, 2018) showed that AimR is a phage-encoded CII/cI-type transcription factor with an N-terminal peptide-binding domain; GMPRGA embeds with high affinity into this pocket, inducing AimR dimerization and restoring repression of the lysis promoter. This revealed a new paradigm of peptide-signal-driven lysogeny decisions at the phage-host interface, analogous to bacterial quorum sensing but acting between viruses and their hosts. This batch is the free-base version: free N-terminal amine and free C-terminal carboxyl with no TFA or other counterion, molecular formula C23H41N9O7S, monoisotopic mass 587.29 Da, average MW 587.70 Da, suitable for cell assays sensitive to TFA residue, crystallography, or in vitro reconstitution requiring precise stoichiometry. As the minimal active motif, GMPRGA is widely used as a tool to study the phage lysogeny-lysis switch, the AimR-AimP signaling axis, structural biology of peptide-repressor recognition, and lysogeny control in phage therapy. Its short length, good water solubility and ease of synthesis make it a convenient probe for phage immunology and synthetic-biology gene-switch applications. | phage biology, lysogeny-lysis decision, Spbeta/spAimR axis, peptide-protein interaction, structural biology probe, synthetic biology switch, phage therapy | Spbeta phage-encoded spAimR (AimR) immune repressor, cI-like transcription factor peptide-binding pocket |
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