Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
PilM/N/O/P proteins form an inner membrane complex that affects the stability of the Pseudomonas aeruginosa type IV pilus secretin.
-
PilM/N/O/P co-fractionate with the inner membrane and are mutually required for stability; the complex is needed for PilQ secretin stability.
"all four proteins, including the nominally cytoplasmic PilM, colocalized to the inner membrane"
Characterization of a five-gene cluster required for the biogenesis of type 4 fimbriae in Pseudomonas aeruginosa.
-
pilM-P transposon and deletion mutants lack functional fimbriae (twitching, phage sensitivity, EM); PilN resembles XpsL and has a hydrophobic segment.
"PilM-P were found to be required for fimbrial biogenesis by complementation studies"
Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable heterodimeric complex.
PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a transenvelope protein interaction network that interacts with PilA.
-
The PilN cytoplasmic tail binds PilM; conserved N-terminal residues are needed for twitching, phage sensitivity and surface PilA.
"the N-terminal cytoplasmic tail of PilN binds to the actin-like protein PilM"
PilN Binding Modulates the Structure and Binding Partners of the Pseudomonas aeruginosa Type IVa Pilus Protein PilM.
-
PilN N-terminal binding monomerises PilM and alters its ATP site.
"upon PilN binding, there is a large domain closure in PilM that alters its ATP binding site"
Type IV Pilus Alignment Subcomplex Proteins PilN and PilO Form Homo- and Heterodimers in Vivo.
-
PilN and PilO form homo- and heterodimers in vivo; certain locked configurations abolish twitching.
"certain covalent homo- or heterodimers eliminated twitching motility, suggesting that specific PilNO configurations are essential for T4P function"
UniProt entry G3XD30 (PILN_PSEAE)