ID   FMM2_NEIGO              Reviewed;         167 AA.
AC   P11764;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Type IV major pilin protein PilE;
DE   AltName: Full=Pilin;
DE   Flags: Precursor;
GN   Name=pilE;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P9-2;
RX   PubMed=2894335; DOI=10.1016/0378-1119(87)90216-2;
RA   Perry A.C.F., Nicholson I.J., Saunders J.R.;
RT   "Structural analysis of the pilE region of Neisseria gonorrhoeae P9.";
RL   Gene 60:85-92(1987).
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; M18245; AAA25473.1; -; Genomic_DNA.
DR   PIR; A29611; A29611.
DR   AlphaFoldDB; P11764; -.
DR   SMR; P11764; -.
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                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024156"
FT   CHAIN           8..167
FT                   /note="Type IV major pilin protein PilE"
FT                   /id="PRO_0000024157"
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        127..160
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   167 AA;  18010 MW;  E8E20659089F78E5 CRC64;
     MNTLQKGFTL IELMIVIAIV GILAAVALPA YQDYTARAQV SEAILLAEGQ KSAVTEYYLN
     HGIWPKDNTS AGVASSSSIK GKYVKEVKVE NGVVTATMNS SNVNKEIQGK KLSLWAKRQD
     GSVKWFCGQP VTRNAKDDTV TADATGNDGK IDTKHLPSTC RDNFDAS