ID   FIMC_PORGN              Reviewed;         453 AA.
AC   O32388;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Major fimbrium subunit FimC {ECO:0000305};
DE   Flags: Precursor;
GN   Name=fimC {ECO:0000312|EMBL:BAA22416.1};
OS   Porphyromonas gingivalis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=837 {ECO:0000312|EMBL:BAA22416.1};
RN   [1] {ECO:0000312|EMBL:BAA22416.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-1703 / FDC 381 {ECO:0000312|EMBL:BAA22416.1};
RX   PubMed=8981345; DOI=10.1111/j.1348-0421.1996.tb01133.x;
RA   Watanabe K., Onoe T., Ozeki M., Shimizu Y., Sakayori T., Nakamura H.,
RA   Yoshimura F.;
RT   "Sequence and product analyses of the four genes downstream from the
RT   fimbrilin gene(fimA) of the oral anaerobe Porphyromonas gingivalis.";
RL   Microbiol. Immunol. 40:725-734(1996).
RN   [2] {ECO:0000312|EMBL:BAA22416.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-1703 / FDC 381 {ECO:0000312|EMBL:BAA22416.1};
RX   PubMed=17526848; DOI=10.1099/mic.0.2006/005561-0;
RA   Nishiyama S., Murakami Y., Nagata H., Shizukuishi S., Kawagishi I.,
RA   Yoshimura F.;
RT   "Involvement of minor components associated with the FimA fimbriae of
RT   Porphyromonas gingivalis in adhesive functions.";
RL   Microbiology 153:1916-1925(2007).
CC   -!- FUNCTION: Minor component of fimbriae. These long, filamentous pili are
CC       attached to the cell surface; they mediate biofilm formation, adhesion
CC       onto host cells and onto other bacteria that are part of the oral
CC       microbiome. They play an important role in invasion of periodontal
CC       tissues and are major virulence factors. FimC, FimD and FimE contribute
CC       to interaction with host CXCR4 and thereby down-regulate the TLR2-
CC       mediated host immune response. {ECO:0000250|UniProtKB:B2RH57}.
CC   -!- SUBUNIT: Fimbriae are composed of a major, structural subunit and the
CC       minor components FimC, FimD and FimE. Identified in a complex composed
CC       of FimC, FimD and FimE (in vitro). The complex interacts with host
CC       extracellular matrix proteins, including fibronectin and type I
CC       collagen. Interacts with host CXCR4. {ECO:0000250|UniProtKB:B2RH57}.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250|UniProtKB:B2RH57}. Cell
CC       outer membrane {ECO:0000250|UniProtKB:B2RH57}. Note=Probably
CC       synthesized as a palmitoylated precursor. Efficient export to the outer
CC       membrane and integration into fimbriae requires lipidation and
CC       subsequent proteolytic removal of the lipidated propeptide. Probably
CC       part of the fimbrium tip, as a part of the complex formed by FimC, FimD
CC       and FimE. {ECO:0000250|UniProtKB:B2RH57}.
CC   -!- MISCELLANEOUS: The name (major fimbrium subunit) does not indicate the
CC       abundance of the protein, but is derived from the greater length of the
CC       major fimbriae. In strain ATCC 33277 and strain ATCC BAA-1703 / FDC
CC       381, major fimbriae are 300 - 1600 nM in length and about 5 nm in
CC       diameter. In contrast, minor fimbriae are only about 80 - 120 nm long.
CC       This length difference is observed only in a small number of strains,
CC       including strain ATCC 33277 and strain ATCC BAA-1703 / FDC 381, and is
CC       due to a loss of function mutation in FimB, a protein that restricts
CC       fimbrial length in other strains. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC       FimA/Mfa1 family. {ECO:0000305}.
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DR   EMBL; D42067; BAA22416.1; -; Genomic_DNA.
DR   RefSeq; WP_039417483.1; NZ_FUFB01000007.1.
DR   AlphaFoldDB; O32388; -.
DR   SMR; O32388; -.
DR   GeneID; 29255428; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009289; C:pilus; ISS:UniProtKB.
DR   GO; GO:0046810; F:host cell extracellular matrix binding; ISS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR   InterPro; IPR029141; FimA_N.
DR   Pfam; PF06321; P_gingi_FimA; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Fimbrium; Lipoprotein; Membrane; Palmitate; Signal;
KW   Virulence.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   PROPEP          29..56
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000436732"
FT   CHAIN           57..453
FT                   /note="Major fimbrium subunit FimC"
FT                   /id="PRO_5004158038"
FT   LIPID           29
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           29
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   453 AA;  50159 MW;  935C2F9D93DFC290 CRC64;
     MKMKYFHHPS GLLPRLLLLL LLTMGAVACT KEDNPDQPTS DEVATVKMSL DDVEMRGGDL
     YSGEDLIKKV RIFVFREGLN GLWVLDKQKL FASGQSDFQN PFTISAHAGP RQIYVIANEP
     DALTTKLDKI LFKKELEDMQ APDVNEPIVR PFTMTGMATA TLNPQGTVQA NISLNRIAAK
     ITLDIKQVTP GSDVIKITKV QILRNAKNSR LLEGTNKPTG YWNWANACDL PLTNNGSAQS
     IIQASAPLYV YENIGSDSDS SGRATQLVVE ALYNGIKTRY YAYVNDKTTT ANHHYSIRRN
     HHYKLDGTIT KMGEFSSLLL TTTVLPWTVE NLDYGFLVPY VAEINPHAVI TQDNVVTFEN
     SLSFTVRIKG RDGSRWKATL DNGLEFGFDS GSAIDGAADG TTVYTIKVKA LKPNGIGIQR
     RTNLFFTVDG KKVILDKNIN PQPTDIKIIQ QGL