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Misaminoacylation of 3,4‐dihydroxyphenylalanine (Dopa) molecules to tRNATyr by endogenous tyrosyl‐tRNA synthetase allowed the quantitative replacement of tyrosine residues with a yield of over 90 % by an in vivo residue‐specific incorporation strategy, to create, for the first time, engineered mussel adhesive proteins (MAPs) in Escherichia coli with a very high Dopa content, close to that of natural MAPs. The Dopa‐incorporated MAPs exhibited a superior surface adhesion and water resistance ability by assistance of Dopa‐mediated interactions including the oxidative Dopa cross‐linking, and furthermore, showed underwater adhesive properties comparable to those of natural MAPs. These results propose promising use of Dopa‐incorporated engineered MAPs as bioglues or adhesive hydrogels for practical underwater applications.

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