{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Schmidt LM"],"funding":["Ministerio de Ciencia, Innovación y Universidades","EMBO","German Research Council"],"pagination":["e0049725"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12918733"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["208(2)"],"pubmed_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 <i>Pseudomonas putida</i> FimV (<i>Pp</i>FimV) with respect to cellular processes involving FimV or HubP in other species. We found that <i>Pp</i>FimV nonspecifically binds to peptidoglycan via its periplasmic LysM domain, which, together with an immunoglobulin-like domain, is necessary for proper polar p"],"journal":["Journal of bacteriology"],"pubmed_title":["Functional characterization of the polar organizer protein FimV in &lt;i&gt;Pseudomonas putida&lt;/i&gt;."],"pmcid":["PMC12918733"],"funding_grant_id":["TH831 10/1","Scientific Exchange Grant 9458","PID2021-126121-NB-I00","PGC2018-097151-B-I00","CEX2020-00108-M"],"pubmed_authors":["Lopez-Sanchez A","Govantes F","Schmidt LM","Treuner-Lange A","Thormann KM","Pulido-Sanchez M","Cava F","Zehner L"],"additional_accession":[]},"is_claimable":false,"name":"Functional characterization of the polar organizer protein FimV in &lt;i&gt;Pseudomonas putida&lt;/i&gt;.","description":"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 <i>Pseudomonas putida</i> FimV (<i>Pp</i>FimV) with respect to cellular processes involving FimV or HubP in other species. We found that <i>Pp</i>FimV nonspecifically binds to peptidoglycan via its periplasmic LysM domain, which, together with an immunoglobulin-like domain, is necessary for proper polar p","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-16T09:17:37.774Z","creation":"2026-07-09T10:46:54.401Z"},"accession":"S-EPMC12918733","cross_references":{"pubmed":["41524594"],"doi":["10.1128/jb.00497-25"]}}