FIME_PORG3
ID FIME_PORG3 Reviewed; 550 AA.
AC B2RH59;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Major fimbrium tip subunit FimE;
DE Flags: Precursor;
GN Name=fimE {ECO:0000312|EMBL:BAG32704.1};
GN OrderedLocusNames=PGN_0185 {ECO:0000312|EMBL:BAG32704.1};
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:BAG32704.1, 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; required for
CC incorporation of FimC and FimD into fimbriae (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, PubMed:19506009). They play an important role in
CC invasion of periodontal tissues and are major virulence factors
CC (Probable). FimC, FimD and FimE contribute to interaction with host
CC CXCR4 and thereby down-regulate the TLR2-mediated host immune response
CC (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,
CC PubMed:19506009). Identified in a complex composed of FimC, FimD and
CC FimE (in vitro) (PubMed:19506009). Does not directly interact with host
CC proteins, but only as a complex with FimC and FimD (PubMed:19506009).
CC {ECO:0000269|PubMed:17526848}.
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 (PubMed:17675496). {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 FimE 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/";
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DR EMBL; AP009380; BAG32704.1; -; Genomic_DNA.
DR RefSeq; WP_012457311.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RH59; -.
DR STRING; 431947.PGN_0185; -.
DR PRIDE; B2RH59; -.
DR EnsemblBacteria; BAG32704; BAG32704; PGN_0185.
DR GeneID; 29255430; -.
DR KEGG; pgn:PGN_0185; -.
DR eggNOG; ENOG5033WW5; Bacteria.
DR HOGENOM; CLU_495072_0_0_10; -.
DR OMA; ELWVFDE; -.
DR BioCyc; PGIN431947:G1G2V-201-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..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 22..51
FT /evidence="ECO:0000255"
FT /id="PRO_0000436743"
FT CHAIN 52..550
FT /note="Major fimbrium tip subunit FimE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5002780248"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 550 AA; 60643 MW; C1B9A6972271998E CRC64;
MKSKSIIAQL LYVLIAFMAV SCVADKSEPC PSGEPTRVSG SIVSLEHHGL RGASADKENS
VERLELWVFD EDGHFLERAV ADLSGSTFTA KIIPSEVERR IHFIANYELA DPSVWVGRSE
REMLPSISVA DDLETIRMWA RISYPSIAPN QNLGQIQLLR NMAKFSLSVT PPAESKLYDA
SYALYNSWNK GTLAPFDPNT GSFPQGQITE PAGVVFANPT SEAAFKEADG AHFFYGFERD
QSNIGTGAGI TCLILKARYN LPNADYTYYK LDFVDTNKVR YNITRNHFYK MILKKAKAPG
RPTLQEALDG AAANNIFLSA EVQALPAFSD GSGMLTVDHT YMVFVQGEPS GTFQATYIPQ
GQNNPDYSKL TVSVSTPTGQ QAAVTSAQHE GNGKIKLTLA QQENLTKRSD VVIGVQGNPD
LKRSVTVLVR EKYQYVFFKA NTSSAENNQV TTQISAGQGN ELLISAKLPD VLNAALLPIT
FKVYTEHFYP KTGGMILGIE GGKTLYKYVL TTMPQNKELQ FRFKSNKVNS AENIAVKMDY
FHDQTIHVTN
