Recombinant E. coli strains and
synthetic protein sequence designs are leveraged for production of disordered polypeptides such as spidroins and
elastin-like peptides (ELPs). These disordered polypeptides, the high-
titer production of which has proven difficult, include repeating structural motifs from a small selection of
amino acid residues, resulting in lack of well-defined
tertiary and
quaternary structure. The recombinant E. coli include expression vectors with genes encoding for the disordered polypeptide product. Expression of these genes is controlled by a
promoter that downregulates and substantially inhibits basal expression in the recombinant
bacteria. Further, the recombinant
bacteria include mutations to one or more stress-response genes from wild-type E. coli, such as yggw, yedv, yedw, yedy, spec, speb, uspc, hcha, loip, mltc, envz, ompr, yhgf, or hupb. The recombinant E. coli enable production of high titers of disordered
protein product while minimizing the toxic effects thereof on the host.