Naturally occurring elastomeric proteins function as molecular springs in their biological settings and show mechanical properties that underlie the elasticity of natural adhesives, cell adhesion proteins and muscle proteins. Constantly subject to repeated stretching-relaxation cycles, many elastomeric proteins demonstrate remarkable consistency and reliability in their mechanical performance. Such properties had hitherto been observed only in naturally evolved elastomeric proteins. Here we use single-molecule atomic force microscopy techniques to demonstrate that an artificial polyprotein made of tandem repeats of non-mechanical protein GB1 has mechanical properties that are comparable or superior to those of known elastomeric proteins. In addition to its mechanical stability, we show that GB1 polyprotein shows a unique combination of mechanical features, including the fastest folding kinetics measured so far for a tethered protein, high folding fidelity, low mechanical fatigue during repeated stretching-relaxation cycles and ability to fold against residual forces. These fine features make GB1 polyprotein an ideal artificial protein-based molecular spring that could function in a challenging working environment requiring repeated stretching-relaxation. This study represents a key step towards engineering artificial molecular springs with tailored nanomechanical properties for bottom-up construction of new devices and materials.