FMA0_DICNO
ID FMA0_DICNO Reviewed; 160 AA.
AC P27688;
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/AC20;
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 AC20;
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}.
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DR EMBL; M37473; AAA23338.1; -; Genomic_DNA.
DR PIR; PS0420; PS0420.
DR AlphaFoldDB; P27688; -.
DR SMR; P27688; -.
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_0000024115"
FT CHAIN 8..160
FT /note="Type IV major fimbrial protein FimA"
FT /id="PRO_0000024116"
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 160 AA; 16693 MW; 55ABC905E5B5057C CRC64;
MKSLQKGFTL IELMIVVAII GILAAFAIPA YNDYIARSQA AEGVSLADGL KVRIAENLQD
GECKGPDADP QSGVVGNEDI GKYALAKIEG DYDASKTDAG APNGCKVEIT YGQGTAEGKI
SKLITGKKLV LDQLVNGSFI AGDGTDLADK FMPNAVKAKK