E6MV22 · FHBP_NEIMH

Function

function

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)

Miscellaneous

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).

Biotechnology

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell outer membrane

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Factor H binding protein
  • Short names
    fHbp
  • Alternative names
    • Genome-derived Neisseria antigen 1870
      (GNA1870
      )
    • Lipoprotein 2086
      (LP2086
      )

Gene names

    • Name
      fhbP
    • ORF names
      NMH_0027

Organism names

Accessions

  • Primary accession
    E6MV22

Proteomes

Subcellular Location

Cell outer membrane
; Lipid-anchor
Note: Surface exposed.

Keywords

Phenotypes & Variants

Disruption phenotype

Bacteria no longer bind fH and are more sensitive to complement-mediated killing.

PTM/Processing

Features

Showing features for signal, lipidation, chain.

TypeIDPosition(s)Description
Signal1-19
Lipidation20N-palmitoyl cysteine
Lipidation20S-diacylglycerol cysteine
ChainPRO_000045508120-274Factor H binding protein

Keywords

Expression

Induction

Expressed at high levels in this strain (at protein level).

Interaction

Subunit

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).

Structure

3D structure databases

Family & Domains

Domain

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.

Sequence similarities

Belongs to the factor H binding-protein family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    274
  • Mass (Da)
    28,990
  • Last updated
    2022-02-23 v2
  • Checksum
    5DDCF683CF877E2A
MNRTAFCCLSLTTALILTACSSGGGGVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTGKLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAKRQFRIGDIAGEHTSFDKLPEGGRATYRGTAFGSDDAGGKLTYTIDFAAKQGNGKIEHLKSPELNVDLAAADIKPDGKRHAVISGSVLYNQAEKGSYSLGIFGGKAQEVAGSAEVKTVNGIRHIGLAAKQ

Sequence caution

The sequence EFV64429.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AEQZ01000011
EMBL· GenBank· DDBJ
EFV64429.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
AY330397
EMBL· GenBank· DDBJ
AAR84472.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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