ID   FMA3_DICNO              Reviewed;         161 AA.
AC   P27689;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Type IV major fimbrial protein FimA;
DE   AltName: Full=Pilin;
DE   AltName: Full=Serogroup B1/AC293;
DE   Flags: Precursor;
GN   Name=fimA;
OS   Dichelobacter nodosus (Bacteroides nodosus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serogroup B1 isolate AC293;
RX   PubMed=1673665; DOI=10.1016/0378-1119(91)90042-a;
RA   Billington S.J., Rood J.I.;
RT   "Sequence of fimbrial subunit-encoding genes from virulent and benign
RT   isolates of Dichelobacter (Bacteroides) nodosus.";
RL   Gene 99:115-119(1991).
CC   -!- FUNCTION: Major component of the type IV fimbriae that plays an
CC       essential role in twitching motility, natural transformation, and
CC       protease secretion. {ECO:0000250|UniProtKB:A5EWR9}.
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 {ECO:0000250|UniProtKB:A5EWR9}. Membrane
CC       {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M37474; AAA23339.1; -; Genomic_DNA.
DR   PIR; PS0421; PS0421.
DR   AlphaFoldDB; P27689; -.
DR   SMR; P27689; -.
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:InterPro.
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   Disulfide bond; Fimbrium; Membrane; Methylation; Transmembrane;
KW   Transmembrane helix.
FT   PROPEP          1..7
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024117"
FT   CHAIN           8..161
FT                   /note="Type IV major fimbrial protein FimA"
FT                   /id="PRO_0000024118"
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   DISULFID        63..105
FT                   /evidence="ECO:0000250|UniProtKB:P02975"
SQ   SEQUENCE   161 AA;  16860 MW;  3F0CF00DBF9EA385 CRC64;
     MKSLQKGFTL IELMIVVAII GILAAFAIPA YNDYIARSQA AEGVSLADGL KVRIAENLQD
     GECKGPDADP QSGVVGNEDK GKYGLAKIEG DYDASKTEAG DPNGCKVEIT YGQGTAGDKI
     SKLITGKKLV LDQLVNGSFV QGDGTDLADK FIPNAVKAKK P