The processed N-terminal portion localizes to the membrane fraction and is probably membrane anchored via lipidation. The C-terminal fragment localizes to the membrane, likely due to the hydrophobic region that is part of the tripartite structure. However, the C-terminal fragment is present in much lower abundance that the full-length protein, possibly due to the degradation of this C-terminal region. The N-terminal region contains several LVIVD repeat domains, which are often found in proteins that localize to the cell surface. The C-terminal region contains a NifU-like domain, originally discovered in proteins involved in nitrogen fixation. Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. Cleaved near the Pro-Gly-Phe (PGF) motif by the archaeosortase ArtA, which recognizes a tripartite structure consisting of a conserved PGF motif, followed by a transmembrane alpha helix domain and a cluster of basic residues. Deletion of the gene does not result in any discernible surface adhesion phenotype under standard conditions and mutant does not exhibit a discernible growth defect. HVO_0405 may be the result of a fusion of two genes, one encoding an ArtA substrate and the second encoding a protein containing a NifU-like domain. As a result of the fusion, the tripartite structure recognized by ArtA is closer to the center of the protein than to the C-terminus. However, despite this atypical localization of the PGF motif, HVO_0405 is indeed processed by ArtA. In the C-terminal section; belongs to the NfuA family.