Pilin-like competence factor, which is essential for natural transformation of the Gram-negative soil bacterium A.baylyi ADP1. Is not a subunit of the pilus structures. Likely functions as a major subunit of an oligomeric structure acting as a channel or pore mediating DNA translocation through the outer membrane and periplasm. The 20-kDa form is present in the cytoplasmic membrane, the periplasm, and the outer membrane, whereas the 23-kDa form is located in the outer membrane and might be due to a further modification. Is maximally expressed in the late stationary growth phase (at protein and mRNA level). Minimal comP expression levels are detected in the middle of the logarithmic growth phase. Glycosylated by PglL2 (PubMed:23658772). The 20-kDa form is glycosylated; a 23-kDa form also exists, that might be due to a further modification. The glycosylation of ComP is not required for its function in DNA binding and uptake (PubMed:10850981). A deletion of comP completely abolishes natural transformation, due to a complete lack of DNA binding and, therefore, uptake of DNA, but has no effect on piliation and on twitching motility. Belongs to the N-Me-Phe pilin family.