ID   FMA1_DICNO              Reviewed;         160 AA.
AC   P17823;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Type IV major fimbrial protein FimA;
DE   AltName: Full=Pilin;
DE   AltName: Full=Serogroup C1;
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 C1 isolate VCS1008;
RX   PubMed=1675419; DOI=10.1111/j.1365-2958.1991.tb00727.x;
RA   Mattick J.S., Anderson B.J., Cox P.T., Dalrymple B.P., Bills M.M.,
RA   Hobbs M., Egerton J.R.;
RT   "Gene sequences and comparison of the fimbrial subunits representative of
RT   Bacteroides nodosus serotypes A to I: class I and class II strains.";
RL   Mol. Microbiol. 5:561-573(1991).
RN   [2]
RP   METHYLATION AT PHE-8, AND DISULFIDE BOND.
RC   STRAIN=Serogroup C isolate 217;
RX   PubMed=2577730; DOI=10.1007/bf01025245;
RA   McKern N.M., Stewart D.J., Strike P.M.;
RT   "Amino acid sequences of pilins from serologically distinct strains of
RT   Bacteroides nodosus.";
RL   J. Protein Chem. 7:157-164(1988).
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}.
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DR   EMBL; X52405; CAA36652.1; -; Genomic_DNA.
DR   PIR; S15260; S15260.
DR   AlphaFoldDB; P17823; -.
DR   SMR; P17823; -.
DR   iPTMnet; P17823; -.
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   1: Evidence at protein level;
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_0000024123"
FT   CHAIN           8..160
FT                   /note="Type IV major fimbrial protein FimA"
FT                   /evidence="ECO:0000269|PubMed:2577730"
FT                   /id="PRO_0000024124"
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                   ECO:0000269|PubMed:2577730"
FT   DISULFID        63..106
FT                   /evidence="ECO:0000269|PubMed:2577730"
SQ   SEQUENCE   160 AA;  16813 MW;  EE1594C1FF78B2D1 CRC64;
     MKSLQKGFTL IELMIVVAII GILAAFAIPA YNDYIARTQV SEGVSLADGL KIRIADNLQD
     GDCTTKGDAS TGEVGNEDKG KYALATIEGT PAANLSELKA EEKNGCLVKI EYGKGTSGGS
     VSALINNTEL VLAQLANGSY VKESATVKDK FLPKALKETK