FHBP_NEIMH
ID FHBP_NEIMH Reviewed; 274 AA.
AC E6MV22;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Factor H binding protein {ECO:0000303|PubMed:16785547};
DE Short=fHbp {ECO:0000303|PubMed:16785547};
DE AltName: Full=Genome-derived Neisseria antigen 1870 {ECO:0000303|PubMed:12642606};
DE Short=GNA1870 {ECO:0000303|PubMed:12642606};
DE AltName: Full=Lipoprotein 2086 {ECO:0000303|PubMed:15039331};
DE Short=LP2086 {ECO:0000303|PubMed:15039331};
DE Flags: Precursor;
GN Name=fhbP; ORFNames=NMH_0027;
OS Neisseria meningitidis serogroup B / serotype 15 (strain H44/76).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=909420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H44/76;
RX PubMed=21378179; DOI=10.1128/jb.01331-10;
RA Piet J.R., Huis In 't Veld R.A., van Schaik B.D., van Kampen A.H., Baas F.,
RA van de Beek D., Pannekoek Y., van der Ende A.;
RT "Genome sequence of Neisseria meningitidis serogroup B strain H44/76.";
RL J. Bacteriol. 193:2371-2372(2011).
RN [2]
RP INDUCTION, AND BIOTECHNOLOGY (VACCINE PRODUCTION).
RC STRAIN=H44/76;
RX PubMed=12642606; DOI=10.1084/jem.20021911;
RA Masignani V., Comanducci M., Giuliani M.M., Bambini S., Adu-Bobie J.,
RA Arico B., Brunelli B., Pieri A., Santini L., Savino S., Serruto D.,
RA Litt D., Kroll S., Welsch J.A., Granoff D.M., Rappuoli R., Pizza M.;
RT "Vaccination against Neisseria meningitidis using three variants of the
RT lipoprotein GNA1870.";
RL J. Exp. Med. 197:789-799(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-274, SUBCELLULAR LOCATION, AND
RP BIOTECHNOLOGY (VACCINE PRODUCTION).
RC STRAIN=H44/76;
RX PubMed=15039331; DOI=10.1128/iai.72.4.2088-2100.2004;
RA Fletcher L.D., Bernfield L., Barniak V., Farley J.E., Howell A., Knauf M.,
RA Ooi P., Smith R.P., Weise P., Wetherell M., Xie X., Zagursky R., Zhang Y.,
RA Zlotnick G.W.;
RT "Vaccine potential of the Neisseria meningitidis 2086 lipoprotein.";
RL Infect. Immun. 72:2088-2100(2004).
RN [4]
RP ERRATUM OF PUBMED:15039331.
RX PubMed=31305626; DOI=10.1128/iai.00212-17;
RA Fletcher L.D., Bernfield L., Barniak V., Farley J.E., Howell A., Knauf M.,
RA Ooi P., Smith R.P., Weise P., Wetherell M., Xie X., Zagursky R., Zhang Y.,
RA Zlotnick G.W.;
RL Infect. Immun. 85:0-0(2017).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HOST FACTOR H,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H44/76;
RX PubMed=16785547; DOI=10.4049/jimmunol.177.1.501;
RA Madico G., Welsch J.A., Lewis L.A., McNaughton A., Perlman D.H.,
RA Costello C.E., Ngampasutadol J., Vogel U., Granoff D.M., Ram S.;
RT "The meningococcal vaccine candidate GNA1870 binds the complement
RT regulatory protein factor H and enhances serum resistance.";
RL J. Immunol. 177:501-510(2006).
CC -!- FUNCTION: A bacterial surface lipoprotein that binds host (human)
CC complement factor H (fH, gene CFH) (PubMed:16785547). Binding
CC contributes to the avoidance of complement-mediated lysis by
CC N.meningitidis (Probable). {ECO:0000269|PubMed:16785547,
CC ECO:0000305|PubMed:16785547}.
CC -!- SUBUNIT: Binds to host factor H (fH from human) (PubMed:16785547). Both
CC fHbp beta-barrels contact Sushi domains 6 and 7 in fH (also called
CC complement control protein domains, CCP). This interaction probably
CC mimics the normal (carbohydrate-dependent) mode of fH recruitement,
CC regulating fH activity (By similarity). {ECO:0000250|UniProtKB:Q9JXV4,
CC ECO:0000269|PubMed:16785547}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:16785547}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}. Note=Surface exposed. {ECO:0000269|PubMed:15039331}.
CC -!- INDUCTION: Expressed at high levels in this strain (at protein level).
CC {ECO:0000269|PubMed:12642606}.
CC -!- DOMAIN: Structures show there are 2 beta barrel domains, 51-156 and
CC 167-274 each form an 8-stranded antiparallel beta-barrel joined by
CC linker between 157-166. {ECO:0000250|UniProtKB:Q9JXV4}.
CC -!- DISRUPTION PHENOTYPE: Bacteria no longer bind fH and are more sensitive
CC to complement-mediated killing. {ECO:0000269|PubMed:16785547}.
CC -!- BIOTECHNOLOGY: Part of an outer membrane vesicle vaccine; antisera
CC against this protein induce efficient complement-mediated killing of
CC the homologous strain. Three antigenic variant groups were detected
CC upon sequencing of group B strains; antibodies against a single variant
CC group provide reduced protection against the other 2 groups.
CC Recombinant protein lipidation increases its immunogenicity.
CC {ECO:0000269|PubMed:12642606, ECO:0000269|PubMed:15039331}.
CC -!- MISCELLANEOUS: One of the major antigens of group B N.meningitidis and
CC a powerful protective antigen. It is highly variable, at least 300
CC protein variants have been seen (see Factor H binding protein sequence
CC typing below). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the factor H binding-protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFV64429.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Factor H binding protein sequence typing;
CC URL="https://pubmlst.org/organisms/neisseria-spp/fhbp/";
CC -!- WEB RESOURCE: Name=Bexsero meningococcal group B Vaccine;
CC URL="https://www.ema.europa.eu/en/medicines/human/EPAR/bexsero";
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DR EMBL; AEQZ01000011; EFV64429.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY330397; AAR84472.1; -; Genomic_DNA.
DR SMR; E6MV22; -.
DR ABCD; E6MV22; 2 sequenced antibodies.
DR EnsemblBacteria; EFV64429; EFV64429; NMH_0027.
DR PATRIC; fig|909420.4.peg.474; -.
DR Proteomes; UP000032707; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR014902; FHBP_C.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR Pfam; PF08794; Lipoprot_C; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Lipoprotein; Membrane; Palmitate; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..274
FT /note="Factor H binding protein"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000455081"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 274 AA; 28990 MW; 5DDCF683CF877E2A CRC64;
MNRTAFCCLS LTTALILTAC SSGGGGVAAD IGAGLADALT APLDHKDKGL QSLTLDQSVR
KNEKLKLAAQ GAEKTYGNGD SLNTGKLKND KVSRFDFIRQ IEVDGQLITL ESGEFQVYKQ
SHSALTAFQT EQIQDSEHSG KMVAKRQFRI GDIAGEHTSF DKLPEGGRAT YRGTAFGSDD
AGGKLTYTID FAAKQGNGKI EHLKSPELNV DLAAADIKPD GKRHAVISGS VLYNQAEKGS
YSLGIFGGKA QEVAGSAEVK TVNGIRHIGL AAKQ
