A bacterial surface lipoprotein that binds host (human) complement factor H (fH, gene CFH) (PubMed:16785547). Binding contributes to the avoidance of complement-mediated lysis by N.meningitidis (Probable). Binds to host factor H (fH from human) (PubMed:16785547). Both fHbp beta-barrels contact Sushi domains 6 and 7 in fH (also called complement control protein domains, CCP). This interaction probably mimics the normal (carbohydrate-dependent) mode of fH recruitement, regulating fH activity (By similarity). Surface exposed. Expressed at high levels in this strain (at protein level). Structures show there are 2 beta barrel domains, 51-156 and 167-274 each form an 8-stranded antiparallel beta-barrel joined by linker between 157-166. Bacteria no longer bind fH and are more sensitive to complement-mediated killing. Part of an outer membrane vesicle vaccine; antisera against this protein induce efficient complement-mediated killing of the homologous strain. Three antigenic variant groups were detected upon sequencing of group B strains; antibodies against a single variant group provide reduced protection against the other 2 groups. Recombinant protein lipidation increases its immunogenicity. One of the major antigens of group B N.meningitidis and a powerful protective antigen. It is highly variable, at least 300 protein variants have been seen (see Factor H binding protein sequence typing below). Belongs to the factor H binding-protein family. Extended N-terminus.