Functional characterization of the polar organizer protein FimV in <i>Pseudomonas putida</i>.

ABSTRACT: Homologs of the polar landmark proteins HubP and FimV are widespread among bacterial species. They all share several common features, including a periplasmic LysM-like domain, a transmembrane region, an extensive cytoplasmic domain enriched in acidic amino acids, and a C-terminal tetrapeptid-repeat (TPR) domain referred to as the FimV domain. Apart from these conserved general features, however, the proteins exhibit little homology across different bacterial genera. Here, we characterized Pseudomonas putida FimV (PpFimV) with respect to cellular processes involving FimV or HubP in other species. We found that PpFimV nonspecifically binds to peptidoglycan via its periplasmic LysM domain, which, together with an immunoglobulin-like domain, is necessary for proper polar p

SUBMITTER: Schmidt LM 

PROVIDER: S-EPMC12918733 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature