ID   FMD3_NEIGO              Reviewed;         180 AA.
AC   Q00046;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 83.
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 D3A;
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; X58404; CAA41303.1; -; Genomic_DNA.
DR   PIR; S15327; S15327.
DR   AlphaFoldDB; Q00046; -.
DR   SMR; Q00046; -.
DR   PRIDE; Q00046; -.
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; Glycoprotein; Membrane;
KW   Methylation; Transmembrane; Transmembrane helix.
FT   PROPEP          1..7
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000024160"
FT   CHAIN           8..180
FT                   /note="Type IV major pilin protein PilE1"
FT                   /id="PRO_0000024161"
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   CARBOHYD        70
FT                   /note="O-linked (GlcNAc...) serine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..160
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   180 AA;  19319 MW;  447ADA0B9263EDB9 CRC64;
     MNTLQKGFTL IELMIVIAIV GILAAVALPA YQDYTARAQV SEAILLAEGQ KSAVTEYYLN
     HGKWPENNTS AGVASPPSDI KGKYVKEVKV ENGVVTATMN SSGVNKEIQG KRLSLWGRRE
     NGSVKWFCGQ PVTRAKADAD ADAAGKDTTN IDTKHLPSTC RDAASAVCIE TPPTAFYKNT