ID   R4X5U1_PORGN            Unreviewed;       383 AA.
AC   R4X5U1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-NOV-2024, entry version 24.
DE   RecName: Full=Fimbrillin {ECO:0000256|ARBA:ARBA00029664};
GN   Name=fimA {ECO:0000313|EMBL:BAN28822.1};
OS   Porphyromonas gingivalis (Bacteroides gingivalis).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=837 {ECO:0000313|EMBL:BAN28822.1};
RN   [1] {ECO:0000313|EMBL:BAN28822.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=19m-1 {ECO:0000313|EMBL:BAN28822.1};
RX   PubMed=23809984; DOI=10.1111/omi.12032;
RA   Nagano K., Abiko Y., Yoshida Y., Yoshimura F.;
RT   "Genetic and antigenic analyses of Porphyromonas gingivalis FimA
RT   fimbriae.";
RL   Mol. Oral. Microbiol. 28:392-403(2013).
CC   -!- FUNCTION: Structural subunit of the major fimbriae. These long,
CC       filamentous pili are attached to the cell surface; they mediate biofilm
CC       formation, adhesion onto host cells and onto other bacteria that are
CC       part of the oral microbiome. They play an important role in the
CC       invasion of periodontal tissues. Fimbriae and their constituents are
CC       major virulence factors. FimA proteins from different strains have
CC       highly divergent sequences, and this has been used for classification.
CC       The sequence-based classification correlates with pathogenicity.
CC       {ECO:0000256|ARBA:ARBA00045723}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000256|ARBA:ARBA00004442}. Fimbrium
CC       {ECO:0000256|ARBA:ARBA00004561}.
CC   -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC       FimA/Mfa1 family. {ECO:0000256|ARBA:ARBA00006011}.
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DR   EMBL; AB795731; BAN28822.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4X5U1; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   FunFam; 2.60.40.2580:FF:000001; Major fimbrium subunit FimA type-2; 1.
DR   FunFam; 2.60.40.3690:FF:000001; Major fimbrium subunit FimA type-4; 1.
DR   Gene3D; 2.60.40.2580; -; 1.
DR   Gene3D; 2.60.40.3690; -; 1.
DR   InterPro; IPR053878; FimA_C.
DR   InterPro; IPR029141; FimA_N.
DR   InterPro; IPR008110; Fimbrillin.
DR   Pfam; PF22492; FimA4_C; 1.
DR   Pfam; PF06321; P_gingi_FimA; 1.
DR   PRINTS; PR01737; FIMBRILLIN.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane {ECO:0000256|ARBA:ARBA00023237};
KW   Fimbrium {ECO:0000256|ARBA:ARBA00023263};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..383
FT                   /note="Fimbrillin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004373084"
FT   DOMAIN          33..168
FT                   /note="Major fimbrial subunit protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06321"
FT   DOMAIN          170..374
FT                   /note="Major fimbrium subunit FimA C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF22492"
SQ   SEQUENCE   383 AA;  41485 MW;  0202408243203CBF CRC64;
     MKKQSFFLLG LAALAMTACN KDNEAEPVTE GNATISVVLK TSNPNRAFGN AGDESKVAKL
     TVMVYNGEQQ EAIESVENAT KVENIKCSAG QRTLVVMANT GEMKLAGKTL AEVKALTTEL
     TAENQEAAGL IMTAEPKTIV LKAGKNYIGY SGTGEGNHIE NDALKIKRVH ARMAFTEIKV
     QMSAAYDNIY TFVPEKIYGL IAKKQSNLFG ATLVNADANY LTGSLTTFNG AYTPTNYANV
     PWLSRDYIAP TADAPQGFYV LENDYSANSG TIHPTILCVY GKLQKNGADL TGTDLAAAQA
     ANWVDGQGKT YYPVLVNFNS NNYTYDNGYT PKNKIERNHK YDIKLTITGP GTNNPENPIT
     ESAHLNVQCT VAEWVLVGQN ATW
//