FMAA_DICNO
ID FMAA_DICNO Reviewed; 158 AA.
AC P02975;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Type IV major fimbrial protein FimA;
DE AltName: Full=198 antigen;
DE AltName: Full=Pilin;
DE AltName: Full=Serogroup A1;
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 A1 isolate 198;
RX PubMed=6094507; DOI=10.1128/jb.160.3.1184-1187.1984;
RA Elleman T.C., Hoyne P.A.;
RT "Nucleotide sequence of the gene encoding pilin of Bacteroides nodosus, the
RT causal organism of ovine footrot.";
RL J. Bacteriol. 160:1184-1187(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serogroup A1 isolate VCS1001;
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 [3]
RP PROTEIN SEQUENCE OF 8-158, AND METHYLATION AT PHE-8.
RC STRAIN=Serogroup A1 isolate 198;
RX PubMed=6653780; DOI=10.1016/0014-5793(83)80039-8;
RA McKern N.M., O'Donnell I.J., Inglis A.S., Stewart D.J., Clark B.L.;
RT "Amino acid sequence of pilin from Bacteroides nodosus (strain 198), the
RT causative organism of ovine footrot.";
RL FEBS Lett. 164:149-153(1983).
RN [4]
RP GLYCOSYLATION.
RX PubMed=17681435; DOI=10.1016/j.vetmic.2007.06.007;
RA Cagatay T.I., Hickford J.G.;
RT "Glycosylation of type-IV fimbriae of Dichelobacter nodosus.";
RL Vet. Microbiol. 126:160-167(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=22027840; DOI=10.1074/jbc.m111.297242;
RA Hartung S., Arvai A.S., Wood T., Kolappan S., Shin D.S., Craig L.,
RA Tainer J.A.;
RT "Ultrahigh resolution and full-length pilin structures with insights for
RT filament assembly, pathogenic functions, and vaccine potential.";
RL J. Biol. Chem. 286:44254-44265(2011).
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 -!- CAUTION: In PubMed:6653780 it is said that 50% of the peptides have N-
CC methyl-Phe and 50% begin with Thr-9. N-terminal methylation produces
CC preview during Edman degradation, which makes this appear to happen
CC when the peptide is completely N-terminally methylated. {ECO:0000305}.
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DR EMBL; K02662; AAA23345.1; -; Genomic_DNA.
DR EMBL; X52403; CAA36648.1; -; Genomic_DNA.
DR EMBL; A00622; CAA00071.1; -; Unassigned_DNA.
DR PIR; A03499; YQBZN.
DR PDB; 3SOK; X-ray; 2.30 A; A/B=8-158.
DR PDBsum; 3SOK; -.
DR AlphaFoldDB; P02975; -.
DR SMR; P02975; -.
DR iPTMnet; P02975; -.
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 3D-structure; Direct protein sequencing; Disulfide bond; Fimbrium;
KW Membrane; Methylation; Transmembrane; Transmembrane helix.
FT PROPEP 1..7
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:6653780"
FT /id="PRO_0000024111"
FT CHAIN 8..158
FT /note="Type IV major fimbrial protein FimA"
FT /id="PRO_0000024112"
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:6653780"
FT DISULFID 63..104
FT /evidence="ECO:0000269|PubMed:22027840"
FT CONFLICT 80
FT /note="G -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 10..49
FT /evidence="ECO:0007829|PDB:3SOK"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:3SOK"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:3SOK"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3SOK"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:3SOK"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:3SOK"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:3SOK"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:3SOK"
FT TURN 121..125
FT /evidence="ECO:0007829|PDB:3SOK"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:3SOK"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3SOK"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3SOK"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3SOK"
SQ SEQUENCE 158 AA; 16863 MW; 1ABC8F21C18339C3 CRC64;
MKSLQKGFTL IELMIVVAII GILAAFAIPA YNDYIARSQA AEGLTLADGL KVRISDHLES
GECKGDANPA SGSLGNDDKG KYALATIDGD YNKDAKTADE KNGCKVVITY GQGTAGEKIS
KLIVGKKLVL DQFVNGSYKY NEGETDLELK FIPNAVKN
