ID   FMD1_NEIGO              Reviewed;         214 AA.
AC   Q00045;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Type IV major pilin protein PilE1;
DE   AltName: Full=L-pilin;
DE   Flags: Precursor;
GN   Name=pilE1;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11 / Isolate D1;
RX   PubMed=1906968; DOI=10.1111/j.1365-2958.1991.tb00766.x;
RA   Manning P.A., Kaufmann A., Roll U., Pohlner J., Meyer T.F., Haas R.;
RT   "L-pilin variants of Neisseria gonorrhoeae MS11.";
RL   Mol. Microbiol. 5:917-926(1991).
CC   -!- FUNCTION: Major component of the type IV pilus (T4P) that plays a role
CC       in cellular adherence, microcolony formation, resistance to neutrophil
CC       mediated killing, twitching motility as well as transformation.
CC       Mediates the attachment and the formation of bacterial microcolonies on
CC       host epithelial cells. Mechanistically, pili retractation induces host
CC       NF-kappa-B activation in infected cells, which is temporally associated
CC       with the formation of gonococcal microcolonies.
CC       {ECO:0000250|UniProtKB:P02974}.
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   -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
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DR   EMBL; X58403; CAA41301.1; -; Genomic_DNA.
DR   PIR; S15326; S15326.
DR   AlphaFoldDB; Q00045; -.
DR   SMR; Q00045; -.
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   3: Inferred from homology;
KW   Cell adhesion; Disulfide bond; Fimbrium; Membrane; Methylation;
KW   Transmembrane; Transmembrane helix.
FT   PROPEP          1..7
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024158"
FT   CHAIN           8..214
FT                   /note="Type IV major pilin protein PilE1"
FT                   /id="PRO_0000024159"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          182..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         8
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT   DISULFID        127..161
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   214 AA;  23021 MW;  AC5D513582CE8030 CRC64;
     MNTLQKGFTL IELMIVIAIV GILAAVALPA YQDYTARAQV SEAILLAEGQ KSAVTEYYLN
     HGIWPENNPA GVASPASDIK GKYVQSVTVA NGVVTAQMKS DGVNKEIKNK KLSLWARREA
     GSVKWFCGQP VTRDNAGTDA VTADTTGKDK EIDTKHLPST CRCFQIGSVK WFCGQPVTRD
     NAGTDAVTAD TTGKDKEIDT KHLPSTCRDK SSAE