Fig. S1. Immunoblotting results, using the antibody against His-tag, of photo-crosslinked protein products of DegP(S210A)His6 variants after being separated by SDS/PAGE.

Fig. S2. Specificities of the anti-OMP antibodies used in this study.

Fig. S3. Coomassie Blue staining results of proteins co-purified with DegP(S210A).

Fig. S4. The OmpC, OmpF and the transmembrane domain of OmpA were captured by DegP(S210A) largely in their unfolded states.

Fig. S5. The degP cells cultured at 44 °C for 6 h are still alive.

Fig. S6. Misfolded OMPs already accumulate in the degP cells under sub-lethal conditions.

Fig. S7. Chaperone function of SurA and protease function of DegP in OMP biogenesis.

Fig. S8. Coomassie Blue staining results of purified SurA, DegP, DegP(S210A) and OmpF, as well as the isolated outer membrane fraction (lacking OmpC and OmpF; at position indicated by the arrow) used in the in vitro refolding/reassembly assay.

Fig. S9. The membrane integrity is impaired in the degP mutant cells cultured at 44 °C.

Fig. S10. Overexpressed DegP(S210A) prevents the toxic accumulation of misfolded OMPs onto the outer membrane but does not refold them.

Doc. S1. Experimental procedures.

Table S1. Abundance of OMPs and other representative envelope proteins in E. coli cells.

Table S2. Relation between misfolded OMPs and growth defect of strains analyzed in this study.

Table S3. E. coli strains used in this study.

Table S4. Plasmids used in this study.

Table S5. Primers used in this study.

Table S6. Antibodies used in this study.

Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.