FIMD_PORG3
ID FIMD_PORG3 Reviewed; 670 AA.
AC B2RH58;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Major fimbrium tip subunit FimD;
DE Flags: Precursor;
GN Name=fimD {ECO:0000312|EMBL:BAG32703.1};
GN OrderedLocusNames=PGN_0184 {ECO:0000312|EMBL:BAG32703.1};
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:BAG32703.1, 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 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: Probably a component of the fimbrium tip (PubMed:17526848,
CC PubMed:19506009). These long, filamentous pili are attached to the cell
CC surface; they mediate biofilm formation, adhesion onto host cells and
CC onto other bacteria that are part of the oral microbiome
CC (PubMed:17526848). They play an important role in invasion of
CC periodontal tissues and are major virulence factors. FimC, FimD and
CC FimE contribute to interaction with host CXCR4 and thereby down-
CC regulate the TLR2-mediated host immune response (PubMed:17675496,
CC PubMed:19506009). {ECO:0000269|PubMed:17526848,
CC ECO:0000269|PubMed:17675496, 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,
CC PubMed:19506009). Identified in a complex composed of FimC, FimD and
CC FimE (in vitro) (PubMed:19506009). The complex interacts with host
CC extracellular matrix proteins, including fibronectin and type I
CC collagen (PubMed:17526848, PubMed:19506009). Interacts with host CXCR4
CC (PubMed:19506009). {ECO:0000269|PubMed:17526848,
CC ECO:0000269|PubMed:19506009}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:17526848}. Cell
CC outer membrane {ECO:0000305}. Note=Probably synthesized as a
CC palmitoylated precursor. Efficient export to the outer membrane and
CC integration into fimbriae requires lipidation and subsequent
CC proteolytic removal of the lipidated propeptide (Probable). Probably
CC part of the fimbrium tip, as a part of the complex formed by FimC, FimD
CC and FimE. {ECO:0000305, 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 FimD family. {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/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009380; BAG32703.1; -; Genomic_DNA.
DR RefSeq; WP_012457310.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RH58; -.
DR SMR; B2RH58; -.
DR STRING; 431947.PGN_0184; -.
DR PRIDE; B2RH58; -.
DR EnsemblBacteria; BAG32703; BAG32703; PGN_0184.
DR GeneID; 29255429; -.
DR KEGG; pgn:PGN_0184; -.
DR eggNOG; ENOG502Z7S7; Bacteria.
DR HOGENOM; CLU_023164_0_0_10; -.
DR OMA; HFYSYYN; -.
DR BioCyc; PGIN431947:G1G2V-200-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 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..24
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 25..50
FT /evidence="ECO:0000255"
FT /id="PRO_0000436739"
FT CHAIN 51..670
FT /note="Major fimbrium tip subunit FimD"
FT /id="PRO_0000436740"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 670 AA; 75848 MW; 29F4CA4D32AD75B1 CRC64;
MRTNRILNII CPPILFLLVG FLFGCVREDI ESDMNETSSL FLQVQPYNQR SEEGGVAAYD
ENTIERLTLV FYKNGTKVWQ AEPVETSPSS NSYYVPVPES MYGQFNGNNS FKIYLVANVN
FSGSFEPNAS ETSFLKTLVP NSILLQNDGK PEDKFAMIGS VEKQINMATS EGKQLGSIEL
KRVAAKLRLK KPVLNISDYE LVGDPKAKFR NCMPKGFLSV EEKPEGVGYE AIDYRPMTEA
NSSVHFYSYY NEWALNNEGR PEFVMMLKLK KTGTDDNTAK PYYYRIPVDG SDKKIRSNHL
YDMAVTIEVL GSLNEEDPVT INGSLSVIEW TSHSDDQTLP DVQYLEVIPQ ETVMNMTTEI
ELDYFSSHSL LPPADVKATC TYVNSNGQQI TDTYTGANVP TVTIDANTKK IKVRSILPIN
NIPKDISFTI KNSIGFEKKI KIRQNPSQFI INTFGTKSSW QPEGNLAPNL NNKAIYQIVV
LSPPADGNMI IGFPPTKEVG FYKKSGSSYT LKHTDRITEQ DEQTANMVSP SFELASQLGA
TLVQDHWEYY TLNPLRLIYH SNQQNRYALM TCAFYWEERK KADGTIERLD DWRLPTRAEI
QLVDKLQREQ AGVVRDIMTG RYYWSGLPDK AIKILLPTAS GNATEQRAHV RCVRDVKNDR
FVKSAKRLKK
