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Table A. Minimal halo-forming concentration (MHC) of truncated variant compared to wild-type KP32gp38. Table B. Enzymatic activity of truncated variants and individual domain(s) of RBP2 (KP32gp38) screened on Klebsiella capsular type collection. Table C. Enzymatic activity of chimeric variants obtained by the fusion of KP32gp38 C-terminal domains with other RBPs with depolymerase activity. Table D. Enzymatic activity of chimeric variants obtained by the fusion of KP32gp38 C-terminal domains with other RBPs with depolymerase activity screened on Klebsiella capsular type collection. Table E. Enzymatic activity of controls of chimeric variants obtained by the reassembly of KP32gp38 and K11gp0043 with position marker (PM) between domains. Table F. Primers used for tile creation of truncated RBPs, together with the tile sequence. Table G. Primers used for tile creation of chimeric RBPs, together with the tile sequence. Table H. Primers used for tile creation of (truncated) RBP fusions with GFP, together with the tile sequence. Table I. Primers used for tile creation to assemble RBP gene clusters of engineered phages (ePs), together with the tile sequence. Table J. Primers for colony PCR, Sanger sequencing and site-directed mutagenesis. Table K. Tile composition of truncated, chimeric and GFP-fused RBPs together with total construct sequence. Table L. The composition of tiles to assemble RBPs gene cluster of engineered phages (ePs). Table M. Primers used for amplification of the KP32 genome fragments (F1-F5). Table N. Components for the preparation of 5X ISO buffer and the Gibson master mix (51) for the assembly of the genomes of the engineered phages. Fig A. Three‑dimensional structures of KP32gp38, its truncated variants, and individual domains predicted using AlphaFold 3 (27). Fig B. Three‑dimensional structures of the wild‑type RBPs used in this study, predicted using AlphaFold 3 (27). Fig C. Three‑dimensional structures of the chimeric RBPs predicted using AlphaFold 3 (27). Fig D. Three‑dimensional structures of the chimeric RBPs (between KP32gp38 and K11gp0043) predicted using AlphaFold 3 (27). Fig E. Fluorescence-based binding assay. Fig F. Three‑dimensional structures GFP-fusions of KP32gp38, its truncated variants, and individual domains predicted using AlphaFold 3 as trimers (27). Fig G. Three‑dimensional structures of KP32gp38, its truncated variants, and individual domains and their GFP-fusions predicted using AlphaFold 3 as monomers (27). Fig H. Graphical abstract. (XLSX)