FIMC_PORG3
ID FIMC_PORG3 Reviewed; 453 AA.
AC B2RH57;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Major fimbrium subunit FimC;
DE Flags: Precursor;
GN Name=fimC {ECO:0000312|EMBL:BAG32702.1};
GN OrderedLocusNames=PGN_0183 {ECO:0000312|EMBL:BAG32702.1};
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1] {ECO:0000312|EMBL:BAG32702.1, ECO:0000312|Proteomes:UP000008842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000312|Proteomes:UP000008842};
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:17675496};
RX PubMed=17675496; DOI=10.4049/jimmunol.179.4.2349;
RA Wang M., Shakhatreh M.A., James D., Liang S., Nishiyama S., Yoshimura F.,
RA Demuth D.R., Hajishengallis G.;
RT "Fimbrial proteins of porphyromonas gingivalis mediate in vivo virulence
RT and exploit TLR2 and complement receptor 3 to persist in macrophages.";
RL J. Immunol. 179:2349-2358(2007).
RN [3]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:17526848};
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).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION IN A COMPLEX CONTAINING
RP FIMC; FIMD AND FIME, INTERACTION WITH HOST CXCR4, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:19506009};
RX PubMed=19506009; DOI=10.1128/iai.00262-09;
RA Pierce D.L., Nishiyama S., Liang S., Wang M., Triantafilou M.,
RA Triantafilou K., Yoshimura F., Demuth D.R., Hajishengallis G.;
RT "Host adhesive activities and virulence of novel fimbrial proteins of
RT Porphyromonas gingivalis.";
RL Infect. Immun. 77:3294-3301(2009).
CC -!- FUNCTION: Minor component of fimbriae (PubMed:17526848). 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 (PubMed:17526848, PubMed:19506009). They
CC play an important role in invasion of periodontal tissues and are major
CC virulence factors (Probable). FimC, FimD and FimE contribute to
CC interaction with host CXCR4 and thereby down-regulate the TLR2-mediated
CC host immune response (PubMed:19506009). {ECO:0000269|PubMed:17526848,
CC ECO:0000269|PubMed:19506009, ECO:0000305}.
CC -!- SUBUNIT: Fimbriae are composed of a major, structural subunit and the
CC minor components FimC, FimD and FimE (PubMed:17526848). Identified in a
CC complex composed of FimC, FimD and FimE (in vitro) (PubMed:19506009).
CC The complex interacts with host extracellular matrix proteins,
CC including fibronectin and type I collagen (PubMed:17526848,
CC PubMed:19506009). Interacts with host CXCR4 (PubMed:19506009).
CC {ECO:0000269|PubMed:17526848, ECO:0000269|PubMed:19506009}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:17526848,
CC ECO:0000269|PubMed:19506009}. Cell outer membrane {ECO:0000305}.
CC Note=Probably synthesized as a palmitoylated precursor. Efficient
CC export to the outer membrane and integration into fimbriae requires
CC lipidation and subsequent proteolytic removal of the lipidated
CC propeptide (Probable). Probably part of the fimbrium tip, as a part of
CC the complex formed by FimC, FimD and FimE. {ECO:0000305,
CC ECO:0000305|PubMed:17675496}.
CC -!- DISRUPTION PHENOTYPE: Triple mutants lacking FimC, FimD and FimE show
CC strongly decreased interaction with host CXCR4 and impaired down-
CC regulation of the TLR2-mediated innate immune response, resulting in
CC strongly reduced survival of the bacteria.
CC {ECO:0000269|PubMed:19506009}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG32702.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A loosening of habits
CC - Issue 182 of August 2016;
CC URL="https://web.expasy.org/spotlight/back_issues/182/";
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DR EMBL; AP009380; BAG32702.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_039417483.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RH57; -.
DR SMR; B2RH57; -.
DR STRING; 431947.PGN_0183; -.
DR PRIDE; B2RH57; -.
DR EnsemblBacteria; BAG32702; BAG32702; PGN_0183.
DR GeneID; 29255428; -.
DR KEGG; pgn:PGN_0183; -.
DR eggNOG; ENOG502ZAVK; Bacteria.
DR HOGENOM; CLU_634398_0_0_10; -.
DR BioCyc; PGIN431947:G1G2V-199-MON; -.
DR Proteomes; UP000008842; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IDA:UniProtKB.
DR GO; GO:0046810; F:host cell extracellular matrix binding; IDA:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB.
DR InterPro; IPR029141; FimA_N.
DR Pfam; PF06321; P_gingi_FimA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
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_0000436731"
FT CHAIN 57..453
FT /note="Major fimbrium subunit FimC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5002781598"
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
