FMM1_NEIMB
ID FMM1_NEIMB Reviewed; 170 AA.
AC P05431;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Fimbrial protein;
DE AltName: Full=Pilin;
DE Flags: Precursor;
GN Name=pilE; OrderedLocusNames=NMB0018;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C311 / Serogroup B;
RX PubMed=3141743; DOI=10.1111/j.1365-2958.1988.tb00073.x;
RA Potts W.J., Saunders J.R.;
RT "Nucleotide sequence of the structural gene for class I pilin from
RT Neisseria meningitidis: homologies with the pilE locus of Neisseria
RT gonorrhoeae.";
RL Mol. Microbiol. 2:647-653(1988).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 8-36, AND METHYLATION AT PHE-8.
RC STRAIN=ATCC 13090;
RX PubMed=413571; DOI=10.1021/bi00596a010;
RA Hermodson M.A., Chen K.C., Buchanan T.M.;
RT "Neisseria pili proteins: amino-terminal amino acid sequences and
RT identification of an unusual amino acid.";
RL Biochemistry 17:442-445(1978).
RN [4]
RP PROTEIN SEQUENCE OF 98-103, PHOSPHORYLATION AT SER-100, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=8645220; DOI=10.1042/bj3160029;
RA Stimson E., Virji M., Barker S., Panico M., Blench I., Saunders J.,
RA Payne G., Moxon E.R., Dell A., Morris H.R.;
RT "Discovery of a novel protein modification: alpha-glycerophosphate is a
RT substituent of meningococcal pilin.";
RL Biochem. J. 316:29-33(1996).
RN [5]
RP FUNCTION, AND GLYCOSYLATION.
RC STRAIN=MC58;
RX PubMed=7934852; DOI=10.1111/j.1365-2958.1993.tb00972.x;
RA Virji M., Saunders J.R., Sims G., Makepeace K., Maskell D., Ferguson D.J.;
RT "Pilus-facilitated adherence of Neisseria meningitidis to human epithelial
RT and endothelial cells: modulation of adherence phenotype occurs
RT concurrently with changes in primary amino acid sequence and the
RT glycosylation status of pilin.";
RL Mol. Microbiol. 10:1013-1028(1993).
RN [6]
RP GLYCOSYLATION AT SER-70, AND STRUCTURE OF CARBOHYDRATE ON SER-70.
RX PubMed=8993351; DOI=10.1111/j.1749-6632.1996.tb52949.x;
RA Virji M., Stimson E., Makepeace K., Dell A., Morris H.R., Payne G.,
RA Saunders J.R., Moxon E.R.;
RT "Posttranslational modifications of meningococcal pili. Identification of a
RT common trisaccharide substitution on variant pilins of strain C311.";
RL Ann. N. Y. Acad. Sci. 797:53-64(1996).
RN [7]
RP GLYCOSYLATION AT SER-70.
RX PubMed=9515697; DOI=10.1046/j.1365-2958.1998.00706.x;
RA Marceau M., Forest K., Beretti J.-L., Tainer J., Nassif X.;
RT "Consequences of the loss of O-linked glycosylation of meningococcal type
RT IV pilin on piliation and pilus-mediated adhesion.";
RL Mol. Microbiol. 27:705-715(1998).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=MC58;
RX PubMed=17121595; DOI=10.1111/j.1365-2958.2006.05448.x;
RA Lappann M., Haagensen J.A., Claus H., Vogel U., Molin S.;
RT "Meningococcal biofilm formation: structure, development and phenotypes in
RT a standardized continuous flow system.";
RL Mol. Microbiol. 62:1292-1309(2006).
RN [9]
RP FUNCTION.
RC STRAIN=8013;
RX PubMed=27698424; DOI=10.1038/ncomms13015;
RA Kolappan S., Coureuil M., Yu X., Nassif X., Egelman E.H., Craig L.;
RT "Structure of the Neisseria meningitidis Type IV pilus.";
RL Nat. Commun. 7:13015-13015(2016).
CC -!- FUNCTION: Major component of the type IV pilus (T4P) that plays a role
CC in cellular adherence, microcolony formation as well as twitching
CC motility. {ECO:0000269|PubMed:17121595, ECO:0000269|PubMed:27698424,
CC ECO:0000269|PubMed:7934852}.
CC -!- SUBUNIT: The pili are polar flexible filaments of about 5.4 nanometers
CC diameter and 2.5 micrometers average length; they consist of only a
CC single polypeptide chain arranged in a helical configuration of five
CC subunits per turn in the assembled pilus.
CC -!- SUBCELLULAR LOCATION: Fimbrium. Membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- PTM: O-linked glycan has been reported to consist either of the
CC Gal(alpha1-3) GlcNAc disaccharide, or the Gal(beta 1-4) Gal(alpha 1-3)
CC 2,4-diacetamido-2,4,6-trideoxyhexose trisaccharide.
CC {ECO:0000269|PubMed:7934852, ECO:0000269|PubMed:9515697}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants are unpiliated but nevertheless
CC form biofilms showing that attachment and accumulation of cells did not
CC depend on pilus expression. {ECO:0000269|PubMed:17121595}.
CC -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
CC -!- CAUTION: In PubMed:413571 it is said that 50% of the peptides have N-
CC methyl-Phe and 50% begin with Thr-9. N-terminal methylation produces
CC preview during Edman degradation, which makes this appear to happen
CC when the peptide is completely N-terminal methylated. {ECO:0000305}.
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DR EMBL; X07731; CAA30557.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF40497.1; -; Genomic_DNA.
DR PIR; F81246; F81246.
DR PIR; S03091; S03091.
DR RefSeq; NP_273084.1; NC_003112.2.
DR RefSeq; WP_010980743.1; NC_003112.2.
DR PDB; 4V1J; X-ray; 1.43 A; A=32-170.
DR PDBsum; 4V1J; -.
DR AlphaFoldDB; P05431; -.
DR SMR; P05431; -.
DR STRING; 122586.NMB0018; -.
DR GlyConnect; 162; 1 O-Linked glycan (1 site).
DR iPTMnet; P05431; -.
DR PaxDb; P05431; -.
DR EnsemblBacteria; AAF40497; AAF40497; NMB0018.
DR KEGG; nme:NMB0018; -.
DR PATRIC; fig|122586.8.peg.24; -.
DR HOGENOM; CLU_091705_4_0_4; -.
DR OMA; VTEYYAT; -.
DR PHI-base; PHI:3826; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR001082; Pilin.
DR InterPro; IPR045584; Pilin-like.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF00114; Pilin; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Direct protein sequencing; Disulfide bond;
KW Fimbrium; Glycoprotein; Membrane; Methylation; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT PROPEP 1..7
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000024164"
FT CHAIN 8..170
FT /note="Fimbrial protein"
FT /id="PRO_0000024165"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 8
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:413571"
FT MOD_RES 100
FT /note="O-(sn-1-glycerophosphoryl)serine"
FT /evidence="ECO:0000269|PubMed:8645220"
FT CARBOHYD 70
FT /note="O-linked (Gal...) serine"
FT /evidence="ECO:0000269|PubMed:8993351,
FT ECO:0000269|PubMed:9515697"
FT /id="CAR_000204"
FT DISULFID 127..163
FT /evidence="ECO:0000250"
FT CONFLICT 97..105
FT /note="QMASSNVNN -> TMLSSGVNK (in Ref. 1; CAA30557)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..155
FT /note="DKAKAANDDVTAAAAANGKKID -> NDTDDTVAAVAADNTGNIN (in
FT Ref. 1; CAA30557)"
FT /evidence="ECO:0000305"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:4V1J"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:4V1J"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:4V1J"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4V1J"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:4V1J"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4V1J"
FT TURN 105..109
FT /evidence="ECO:0007829|PDB:4V1J"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:4V1J"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:4V1J"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4V1J"
SQ SEQUENCE 170 AA; 18072 MW; 037368DD1B26FA6F CRC64;
MNTLQKGFTL IELMIVIAIV GILAAVALPA YQDYTARAQV SEAILLAEGQ KSAVTEYYLN
HGEWPGNNTS AGVATSSEIK GKYVKSVEVK NGVVTAQMAS SNVNNEIKGK KLSLWAKRQN
GSVKWFCGQP VTRDKAKAAN DDVTAAAAAN GKKIDTKHLP STCRDASDAS
