ID   FMM1_NEIMA              Reviewed;         170 AA.
AC   P57039; A1IPB0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Fimbrial protein;
DE   AltName: Full=Pilin;
DE   Flags: Precursor;
GN   Name=pilE; OrderedLocusNames=NMA0264;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
RN   [2]
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).
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:0000250|UniProtKB:P05431}.
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 consists of GlcNAc-Gal disaccharide.
CC       {ECO:0000269|PubMed:9515697}.
CC   -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
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DR   EMBL; AL157959; CAM07570.1; -; Genomic_DNA.
DR   PIR; D82021; D82021.
DR   RefSeq; WP_010981065.1; NC_003116.1.
DR   AlphaFoldDB; P57039; -.
DR   SMR; P57039; -.
DR   iPTMnet; P57039; -.
DR   EnsemblBacteria; CAM07570; CAM07570; NMA0264.
DR   KEGG; nma:NMA0264; -.
DR   HOGENOM; CLU_091705_4_0_4; -.
DR   OMA; VTEYYAT; -.
DR   BioCyc; NMEN122587:NMA_RS01390-MON; -.
DR   Proteomes; UP000000626; 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   Cell adhesion; Disulfide bond; Fimbrium; Glycoprotein; Membrane;
KW   Methylation; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   PROPEP          1..7
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000024162"
FT   CHAIN           8..170
FT                   /note="Fimbrial protein"
FT                   /id="PRO_0000024163"
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   MOD_RES         100
FT                   /note="O-(sn-1-glycerophosphoryl)serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        70
FT                   /note="O-linked (Gal...) serine"
FT                   /evidence="ECO:0000269|PubMed:9515697"
FT   DISULFID        127..163
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   170 AA;  18134 MW;  1C59E6CA81614596 CRC64;
     MNTLQKGFTL IELMIVIAIV GILAAVALPA YQDYTARAQV SEAILLAEGQ KSAVTEYYLN
     HGEWPSNNTS AGVASSTDIK GKYVQSVEVK NGVVTATMAS SNVNNEIKGK KLSLWAKRQD
     GSVKWFCGQP VKRNDTATTN DDVKADTAAN GKQIDTKHLP STCRDAASAG