ID   FIME_PORGN              Reviewed;         550 AA.
AC   O32390;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Major fimbrium tip subunit FimE;
DE   Flags: Precursor;
GN   Name=fimE {ECO:0000312|EMBL:BAA22418.2};
OS   Porphyromonas gingivalis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=837 {ECO:0000312|EMBL:BAA22418.2};
RN   [1] {ECO:0000312|EMBL:BAA22418.2}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-1703 / FDC 381 {ECO:0000312|EMBL:BAA22418.2};
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:BAA22418.2}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-1703 / FDC 381 {ECO:0000312|EMBL:BAA22418.2};
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: Probably a component of the fimbrium tip; required for
CC       incorporation of FimC and FimD into fimbriae. These long, filamentous
CC       pili are attached to the cell surface; they mediate biofilm formation,
CC       adhesion onto host cells and onto other bacteria that are part of the
CC       oral 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:B2RH59}.
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). Does not directly interact with host
CC       proteins, but only as a complex with FimC and FimD.
CC       {ECO:0000250|UniProtKB:B2RH59}.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250|UniProtKB:B2RH59}. Cell
CC       outer membrane {ECO:0000250|UniProtKB:B2RH59}. 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 (Probable).
CC       Probably part of the fimbrium tip, as a part of the complex formed by
CC       FimC, FimD and FimE (By similarity). {ECO:0000250|UniProtKB:B2RH59,
CC       ECO:0000305}.
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}.
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DR   EMBL; D42067; BAA22418.2; -; Genomic_DNA.
DR   RefSeq; WP_012457311.1; NZ_FUFB01000007.1.
DR   AlphaFoldDB; O32390; -.
DR   GeneID; 29255430; -.
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   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
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_0000436744"
FT   CHAIN           52..550
FT                   /note="Major fimbrium tip subunit FimE"
FT                   /id="PRO_5004158230"
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