Gene Ontology annotation through association of InterPro records with GO terms
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.
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PilM/N/O/P form an inner-membrane complex; PilM co-fractionates with the inner membrane; loss of one component reduces the others and destabilises PilQ.
"Stability studies via Western blot analyses revealed that loss of one component has a negative impact on the levels of other members of the putative complex."
Characterization of a five-gene cluster required for the biogenesis of type 4 fimbriae in Pseudomonas aeruginosa.
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Transposon and deletion mutants of pilM-P lack functional fimbriae (twitching, phage sensitivity, EM); PilM resembles FtsA/MreB/actin.
"PilM-P were found to be required for fimbrial biogenesis by complementation studies"
PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a transenvelope protein interaction network that interacts with PilA.
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The cytoplasmic N-terminal tail of PilN binds PilM, linking the cytoplasm to the PilNOPQ transenvelope complex.
"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.
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PilM structures with ATP; PilN binding monomerises PilM and alters the ATP site; PilM binds PilB and PilT directly and PilC by two-hybrid.
"Pull-down experiments demonstrated direct interactions of PilM with PilB and PilT."
Structure of the PilM-PilN inner membrane type IV pilus biogenesis complex from Thermus thermophilus.
The Type IV Pilus Assembly ATPase PilB of Myxococcus xanthus Interacts with the Inner Membrane Platform Protein PilC and the Nucleotide-binding Protein PilM.
Type IV Pilus Alignment Subcomplex Proteins PilN and PilO Form Homo- and Heterodimers in Vivo.
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PilM is required for in vivo PilNO heterodimer formation.
"Deletion of genes encoding alignment subcomplex components, PilM or PilP, but not other T4P components, including the motor ATPases PilB or PilT, blocked in vivo formation of disulfide-bonded PilNO heterodimers"
UniProt entry G3XD28 (PILM_PSEAE)