FMAJ_DICNO
ID FMAJ_DICNO Reviewed; 160 AA.
AC P19528;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Type IV major fimbrial protein FimA;
DE AltName: Full=351 antigen;
DE AltName: Full=Pilin;
DE AltName: Full=Serogroup H;
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 H isolate 351;
RX PubMed=2621448; DOI=10.1099/00221287-135-5-1113;
RA Hoyne P.A., Elleman T.C., McKern N.M., Stewart D.J.;
RT "Sequence of pilin from Bacteroides nodosus 351 (Serogroup H) and
RT implications for serogroup classification.";
RL J. Gen. Microbiol. 135:1113-1122(1989).
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; M26980; AAA23336.1; -; Genomic_DNA.
DR PIR; A37167; A37167.
DR AlphaFoldDB; P19528; -.
DR SMR; P19528; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR InterPro; IPR000983; Bac_GSPG_pilin.
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 PRINTS; PR00813; BCTERIALGSPG.
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 Fimbrium; Membrane; Methylation; Transmembrane; Transmembrane helix.
FT PROPEP 1..7
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000024140"
FT CHAIN 8..160
FT /note="Type IV major fimbrial protein FimA"
FT /id="PRO_0000024141"
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"
SQ SEQUENCE 160 AA; 17170 MW; 3160DAEAFE87ABAA CRC64;
MKSLQKGFTL IELMIVVAII GILAAIAIPQ YQNYIARSQV SRVMSETGQM RTAIETCLLD
GKKADECFIG WTKSNLLGAS GSPSSSNDST ADHPGQGGLV IDYKLEADAT NAITATFGQN
AAATLHGKAL KWTRDPKATW SCSTDVELKF RPTGCKDDLK