FHBP_NEIMB
ID FHBP_NEIMB Reviewed; 274 AA.
AC Q9JXV4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 118.
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;
DE Short=LP2086 {ECO:0000303|PubMed:15039331};
DE Flags: Precursor;
GN Name=fhbP; OrderedLocusNames=NMB1870;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION TO N-TERMINUS,
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, PROBABLE PALMITOYLATION AT
RP CYS-20, AND BIOTECHNOLOGY.
RC STRAIN=MC58;
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 BIOTECHNOLOGY (VACCINE PRODUCTION).
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 ANTIGENICITY, AND DOMAIN.
RC STRAIN=MC58;
RX PubMed=15664958; DOI=10.1128/iai.73.2.1151-1160.2005;
RA Giuliani M.M., Santini L., Brunelli B., Biolchi A., Arico B.,
RA Di Marcello F., Cartocci E., Comanducci M., Masignani V., Lozzi L.,
RA Savino S., Scarselli M., Rappuoli R., Pizza M.;
RT "The region comprising amino acids 100 to 255 of Neisseria meningitidis
RT lipoprotein GNA 1870 elicits bactericidal antibodies.";
RL Infect. Immun. 73:1151-1160(2005).
RN [6]
RP FUNCTION, AND BACTERIAL FACTOR H-BINDING.
RC STRAIN=MC58;
RX PubMed=16751403; DOI=10.4049/jimmunol.176.12.7566;
RA Schneider M.C., Exley R.M., Chan H., Feavers I., Kang Y.H., Sim R.B.,
RA Tang C.M.;
RT "Functional significance of factor H binding to Neisseria meningitidis.";
RL J. Immunol. 176:7566-7575(2006).
RN [7]
RP INTERACTION WITH HOST FACTOR H, AND DISRUPTION PHENOTYPE.
RC STRAIN=MC58;
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).
RN [8]
RP BIOTECHNOLOGY.
RX PubMed=16825336; DOI=10.1073/pnas.0603940103;
RA Giuliani M.M., Adu-Bobie J., Comanducci M., Arico B., Savino S.,
RA Santini L., Brunelli B., Bambini S., Biolchi A., Capecchi B., Cartocci E.,
RA Ciucchi L., Di Marcello F., Ferlicca F., Galli B., Luzzi E., Masignani V.,
RA Serruto D., Veggi D., Contorni M., Morandi M., Bartalesi A., Cinotti V.,
RA Mannucci D., Titta F., Ovidi E., Welsch J.A., Granoff D., Rappuoli R.,
RA Pizza M.;
RT "A universal vaccine for serogroup B meningococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10834-10839(2006).
RN [9] {ECO:0007829|PDB:1YS5}
RP STRUCTURE BY NMR OF 120-274, AND DOMAIN.
RC STRAIN=MC58;
RX PubMed=16407174; DOI=10.1074/jbc.m508595200;
RA Cantini F., Savino S., Scarselli M., Masignani V., Pizza M., Romagnoli G.,
RA Swennen E., Veggi D., Banci L., Rappuoli R.;
RT "Solution structure of the immunodominant domain of protective antigen
RT GNA1870 of Neisseria meningitidis.";
RL J. Biol. Chem. 281:7220-7227(2006).
RN [10] {ECO:0007744|PDB:2W80, ECO:0007744|PDB:2W81}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 25-274 IN COMPLEX WITH HUMAN
RP COMPLEMENT FACTOR H, FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF GLU-237
RP AND GLU-258.
RX PubMed=19225461; DOI=10.1038/nature07769;
RA Schneider M.C., Prosser B.E., Caesar J.J., Kugelberg E., Li S., Zhang Q.,
RA Quoraishi S., Lovett J.E., Deane J.E., Sim R.B., Roversi P., Johnson S.,
RA Tang C.M., Lea S.M.;
RT "Neisseria meningitidis recruits factor H using protein mimicry of host
RT carbohydrates.";
RL Nature 458:890-893(2009).
RN [11] {ECO:0007744|PDB:2Y7S}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 27-274, FUNCTION, DOMAIN,
RP BIOTECHNOLOGY, AND MUTAGENESIS OF 153-ILE--THR-170; 192-ALA-ALA-193;
RP 211-ASP--ALA-236 AND LYS-249.
RC STRAIN=MC58;
RX PubMed=21753121; DOI=10.1126/scitranslmed.3002234;
RA Scarselli M., Arico B., Brunelli B., Savino S., Di Marcello F., Palumbo E.,
RA Veggi D., Ciucchi L., Cartocci E., Bottomley M.J., Malito E., Lo Surdo P.,
RA Comanducci M., Giuliani M.M., Cantini F., Dragonetti S., Colaprico A.,
RA Doro F., Giannetti P., Pallaoro M., Brogioni B., Tontini M.,
RA Hilleringmann M., Nardi-Dei V., Banci L., Pizza M., Rappuoli R.;
RT "Rational design of a meningococcal antigen inducing broad protective
RT immunity.";
RL Sci. Transl. Med. 3:91ra62-91ra62(2011).
RN [12] {ECO:0007744|PDB:4AYD, ECO:0007744|PDB:4AYE}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 27-274 IN COMPLEX WITH HUMAN
RP COMPLEMENT FACTOR H, FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF GLU-237
RP AND GLU-258.
RX PubMed=23133374; DOI=10.1371/journal.ppat.1002981;
RA Johnson S., Tan L., van der Veen S., Caesar J., Goicoechea De Jorge E.,
RA Harding R.J., Bai X., Exley R.M., Ward P.N., Ruivo N., Trivedi K.,
RA Cumber E., Jones R., Newham L., Staunton D., Ufret-Vincenty R., Borrow R.,
RA Pickering M.C., Lea S.M., Tang C.M.;
RT "Design and evaluation of meningococcal vaccines through structure-based
RT modification of host and pathogen molecules.";
RL PLoS Pathog. 8:E1002981-E1002981(2012).
RN [13] {ECO:0007744|PDB:2YPV}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 23-274.
RX PubMed=23396847; DOI=10.1073/pnas.1222845110;
RA Malito E., Faleri A., Lo Surdo P., Veggi D., Maruggi G., Grassi E.,
RA Cartocci E., Bertoldi I., Genovese A., Santini L., Romagnoli G.,
RA Borgogni E., Brier S., Lo Passo C., Domina M., Castellino F., Felici F.,
RA van der Veen S., Johnson S., Lea S.M., Tang C.M., Pizza M., Savino S.,
RA Norais N., Rappuoli R., Bottomley M.J., Masignani V.;
RT "Defining a protective epitope on factor H binding protein, a key
RT meningococcal virulence factor and vaccine antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3304-3309(2013).
RN [14] {ECO:0007744|PDB:5T5F}
RP X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) OF 23-274.
RX PubMed=27784765; DOI=10.1042/bcj20160806;
RA Malito E., Lo Surdo P., Veggi D., Santini L., Stefek H., Brunelli B.,
RA Luzzi E., Bottomley M.J., Beernink P.T., Scarselli M.;
RT "Neisseria meningitidis factor H-binding protein bound to monoclonal
RT antibody JAR5: implications for antibody synergy.";
RL Biochem. J. 473:4699-4713(2016).
RN [15] {ECO:0007744|PDB:5O14}
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 27-274.
RX PubMed=29410413; DOI=10.1038/s41467-018-02827-7;
RA Lopez-Sagaseta J., Beernink P.T., Bianchi F., Santini L., Frigimelica E.,
RA Lucas A.H., Pizza M., Bottomley M.J.;
RT "Crystal structure reveals vaccine elicited bactericidal human antibody
RT targeting a conserved epitope on meningococcal fHbp.";
RL Nat. Commun. 9:528-528(2018).
RN [16] {ECO:0007744|PDB:5NQX, ECO:0007744|PDB:5NQZ}
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 27-274.
RX PubMed=29535307; DOI=10.1038/s41467-018-03146-7;
RA Hollingshead S., Jongerius I., Exley R.M., Johnson S., Lea S.M., Tang C.M.;
RT "Structure-based design of chimeric antigens for multivalent protein
RT vaccines.";
RL Nat. Commun. 9:1051-1051(2018).
RN [17] {ECO:0007744|PDB:6XZW}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 27-274.
RX PubMed=33007046; DOI=10.1371/journal.ppat.1008882;
RA Veggi D., Bianchi F., Santini L., Lo Surdo P., Chesterman C.C.,
RA Pansegrau W., Bechi N., Huang Y., Masignani V., Pizza M., Rappuoli R.,
RA Bottomley M.J., Cozzi R., Maione D.;
RT "4CMenB vaccine induces elite cross-protective human antibodies that
RT compete with human factor H for binding to meningococcal fHbp.";
RL PLoS Pathog. 16:e1008882-e1008882(2020).
CC -!- FUNCTION: A bacterial surface lipoprotein that binds host (human)
CC complement factor H (fH, gene CFH), binding contributes to the
CC avoidance of complement-mediated lysis by N.meningitidis. Binding of fH
CC to the bacteria surface is independent of bacterial sialic acid
CC moieties (PubMed:16751403). fH binding affinity is high enough that it
CC may sequester plasma fH, depleting its circulating levels and de-
CC regulating complement in the host (Probable). This protein induces high
CC levels of bactericidal antibodies in mice (PubMed:12642606,
CC PubMed:15039331, PubMed:15664958, PubMed:21753121, PubMed:23133374).
CC {ECO:0000269|PubMed:12642606, ECO:0000269|PubMed:15039331,
CC ECO:0000269|PubMed:15664958, ECO:0000269|PubMed:16751403,
CC ECO:0000269|PubMed:21753121, ECO:0000269|PubMed:23133374,
CC ECO:0000305|PubMed:19225461}.
CC -!- SUBUNIT: Binds to host factor H (fH from human) (PubMed:16751403,
CC PubMed:16785547, PubMed:19225461, PubMed:23133374). Both fHbp beta-
CC barrels contact Sushi domains 6 and 7 in fH (also called complement
CC control protein domains, CCP). This interaction probably mimics the
CC normal (carbohydrate-dependent) mode of fH recruitement, regulating fH
CC activity. Sucrose octasulphate inhibits the fHbp-fH interaction
CC (PubMed:16785547, PubMed:19225461, PubMed:23133374).
CC {ECO:0000269|PubMed:16751403, ECO:0000269|PubMed:16785547,
CC ECO:0000269|PubMed:19225461, ECO:0000269|PubMed:23133374}.
CC -!- INTERACTION:
CC Q9JXV4; P08603: CFH; Xeno; NbExp=6; IntAct=EBI-15758684, EBI-1223708;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:12642606}; Lipid-anchor
CC {ECO:0000305|PubMed:12642606}. Secreted {ECO:0000269|PubMed:12642606}.
CC Extracellular vesicle, bacterial extracellular vesicle
CC {ECO:0000269|PubMed:12642606}. Note=Surface exposed on encapsulated and
CC non-encapsulated strains. In freshly innoculated cells no secreted
CC protein is seen, as cultures grow the amount of protein in the cell
CC supernatant increases. {ECO:0000269|PubMed:12642606}.
CC -!- INDUCTION: The amount of protein increases as cells approach stationary
CC phase (at protein level). {ECO:0000269|PubMed:12642606}.
CC -!- DOMAIN: Divided into 3 domains by antibody recognition; domain A (27-
CC 119), domain B (120-183) and domain C (184-274). Domain A contains
CC linear epitopes that are common to the three GNA 1870 (fHbp) variants,
CC antibodies against it recognize N.meningitidis cells. Domain B contains
CC linear epitopes common to variant 1 proteins but antibodies against it
CC do not give a robust signal against N.meningitidis cells. Domain C does
CC not have linear epitopes but antibodies against it recognize
CC N.meningitidis cells. Bactericidal antibodies are directed against
CC conformational epitopes located in the BC domain (PubMed:15664958).
CC Structures show there are 2 beta barrel domains, 51-156 and 167-274
CC each form an 8-stranded antiparallel beta-barrel joined by linker
CC between 157-166 (PubMed:16407174, PubMed:19225461, PubMed:21753121).
CC {ECO:0000269|PubMed:15664958, ECO:0000269|PubMed:16407174,
CC ECO:0000269|PubMed:19225461, ECO:0000269|PubMed:21753121}.
CC -!- PTM: Protein is lipidated in N.meningitidis upon growth in radioactive
CC palmitic acid, probably on Cys-20. {ECO:0000269|PubMed:12642606}.
CC -!- DISRUPTION PHENOTYPE: Bacteria are more sensitive to complement-
CC 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. Thus
CC inclusion of an example of each in a vaccine may provide adequate
CC protection against all strains. Recombinant protein lipidation
CC increases its immunogenicity (PubMed:12642606, PubMed:15039331). This
CC is the variant used in the 5CVMB vaccine (PubMed:16825336). Engineering
CC fHbp to include the antigenic epitopes of the 3 main group variants to
CC produce a single protein for vaccine production has lead to a molecule
CC with increased antigenic efficacy. This G1 variant has 23 changes
CC compared to the MC58 standard; its X-ray structure is reported
CC (PubMed:21753121). {ECO:0000269|PubMed:12642606,
CC ECO:0000269|PubMed:15039331, ECO:0000269|PubMed:16825336,
CC ECO:0000269|PubMed:21753121, ECO:0007744|PDB:2Y7S}.
CC -!- MISCELLANEOUS: One of the major antigens of group B N.meningitidis and
CC a powerful protective antigen. It is highly variable, over 300 protein
CC variants have been seen (see Factor H binding protein sequence typing
CC website). The protein in strain MC58 is called V1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the factor H binding-protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF42204.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305|PubMed:12642606};
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; AE002098; AAF42204.1; ALT_INIT; Genomic_DNA.
DR PIR; D81032; D81032.
DR RefSeq; NP_274866.1; NC_003112.2.
DR RefSeq; WP_010981001.1; NC_003112.2.
DR PDB; 1YS5; NMR; -; A=120-274.
DR PDB; 2W80; X-ray; 2.35 A; C/D/F/H=25-274.
DR PDB; 2W81; X-ray; 2.35 A; C/D/F=25-274.
DR PDB; 2Y7S; X-ray; 1.90 A; A/B=27-274.
DR PDB; 2YPV; X-ray; 1.80 A; A=23-274.
DR PDB; 4AYD; X-ray; 2.40 A; C/D/F=27-274.
DR PDB; 4AYE; X-ray; 2.80 A; C/D/F=27-274.
DR PDB; 5NQX; X-ray; 3.66 A; A/B/C/D/E=26-247, A/B/C/D/E=249-274.
DR PDB; 5NQZ; X-ray; 1.63 A; A/B=27-274.
DR PDB; 5O14; X-ray; 2.19 A; A/B=27-274.
DR PDB; 5T5F; X-ray; 2.98 A; A=23-274.
DR PDB; 6XZW; X-ray; 2.40 A; D=27-274.
DR PDB; 7KET; X-ray; 2.00 A; C=20-274.
DR PDB; 7LCV; X-ray; 1.70 A; C=20-274.
DR PDBsum; 1YS5; -.
DR PDBsum; 2W80; -.
DR PDBsum; 2W81; -.
DR PDBsum; 2Y7S; -.
DR PDBsum; 2YPV; -.
DR PDBsum; 4AYD; -.
DR PDBsum; 4AYE; -.
DR PDBsum; 5NQX; -.
DR PDBsum; 5NQZ; -.
DR PDBsum; 5O14; -.
DR PDBsum; 5T5F; -.
DR PDBsum; 6XZW; -.
DR PDBsum; 7KET; -.
DR PDBsum; 7LCV; -.
DR SMR; Q9JXV4; -.
DR DIP; DIP-59745N; -.
DR IntAct; Q9JXV4; 1.
DR PaxDb; Q9JXV4; -.
DR ABCD; Q9JXV4; 13 sequenced antibodies.
DR EnsemblBacteria; AAF42204; AAF42204; NMB1870.
DR KEGG; nme:NMB1870; -.
DR PATRIC; fig|122586.8.peg.2390; -.
DR HOGENOM; CLU_086005_0_0_4; -.
DR OMA; PLDHKDK; -.
DR EvolutionaryTrace; Q9JXV4; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0097691; C:bacterial extracellular vesicle; IEA:UniProtKB-SubCell.
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 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..274
FT /note="Factor H binding protein"
FT /id="PRO_0000455080"
FT REGION 27..119
FT /note="Domain A"
FT /evidence="ECO:0000269|PubMed:15664958"
FT REGION 120..183
FT /note="Domain B"
FT /evidence="ECO:0000269|PubMed:15664958"
FT REGION 184..274
FT /note="Domain C"
FT /evidence="ECO:0000269|PubMed:15664958"
FT SITE 223
FT /note="Important for antibody recognition"
FT /evidence="ECO:0000305|PubMed:15664958"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000305|PubMed:12642606"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 153..170
FT /note="IAGEHTSFDKLPEGGRAT->LGGEHTAFNQLPDGKAE: Increased
FT vaccine efficacy (G1 variant); when associated with 192-T-
FT K-193, 211-E--E-236 and R-249."
FT /evidence="ECO:0000269|PubMed:21753121"
FT MUTAGEN 192..193
FT /note="AA->TK: Increased vaccine efficacy (G1 variant);
FT when associated with 153-L--E-170, 211-E--E-236 and R-249."
FT /evidence="ECO:0000269|PubMed:21753121"
FT MUTAGEN 211..236
FT /note="DLAAADIKPDGKRHAVISGSVLYNQA->ELASAEIKADGKSHAVILGDVRYG
FT SE: Increased vaccine efficacy (G1 variant); when
FT associated with 153-L--E-170, 192-T-K-193 and R-249."
FT /evidence="ECO:0000269|PubMed:21753121"
FT MUTAGEN 237
FT /note="E->A: 7-fold decreased binding to fH. No longer
FT binds fH; when associated with A-258."
FT /evidence="ECO:0000269|PubMed:19225461,
FT ECO:0000269|PubMed:23133374"
FT MUTAGEN 249
FT /note="K->R: Increased vaccine efficacy (G1 variant); when
FT associated with 153-L--E-170, 192-T-K-193 and 211-E--E-
FT 236."
FT /evidence="ECO:0000269|PubMed:21753121"
FT MUTAGEN 258
FT /note="E->A: 150-fold decreased binding to fH. No longer
FT binds fH; when associated with A-237."
FT /evidence="ECO:0000269|PubMed:19225461,
FT ECO:0000269|PubMed:23133374"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:5NQZ"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:7KET"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2W81"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:7LCV"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2W80"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 91..103
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 106..119
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 121..134
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 142..155
FT /evidence="ECO:0007829|PDB:5NQZ"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 180..190
FT /evidence="ECO:0007829|PDB:5NQZ"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:5NQZ"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 236..247
FT /evidence="ECO:0007829|PDB:5NQZ"
FT STRAND 252..273
FT /evidence="ECO:0007829|PDB:5NQZ"
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
