This lecture explores the Hsp90 and Hsp70 chaperones in the aquatic bacteria Shewanella oneidensis, highlighting their role in protein quality control, client identification, and proteostasis control. The instructor discusses the essentiality of Hsp90 at high temperatures, its ATPase activity, and its collaboration with Hsp70. The physiological roles of bacterial Hsp90, its function in stress response, and its impact on protein aggregation are also covered. Additionally, the lecture delves into the interaction between bacterial Hsp90 and Hsp70, the structure of the Hsp90 chaperone, and the importance of cochaperones and client proteins. Furthermore, the lecture presents the role of TilS and the JDP cochaperone AtcJ in cold adaptation in S. oneidensis, shedding light on their functions and interactions within the bacterial cell.