ID   FIMD_PORGN              Reviewed;         670 AA.
AC   O32389;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Major fimbrium tip subunit FimD;
DE   Flags: Precursor;
GN   Name=fimD {ECO:0000312|EMBL:BAA22417.1};
OS   Porphyromonas gingivalis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=837 {ECO:0000312|EMBL:BAA22417.1};
RN   [1] {ECO:0000312|EMBL:BAA22417.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-1703 / FDC 381 {ECO:0000312|EMBL:BAA22417.1};
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:BAA22417.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-1703 / FDC 381 {ECO:0000312|EMBL:BAA22417.1};
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: Probably a component of the fimbrium tip. 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. 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.
CC       {ECO:0000250|UniProtKB:B2RH58}.
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:B2RH58}.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250|UniProtKB:B2RH58}. Cell
CC       outer membrane {ECO:0000250|UniProtKB:B2RH58}. 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. {ECO:0000250|UniProtKB:B2RH58, 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 FimD family. {ECO:0000305}.
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DR   EMBL; D42067; BAA22417.1; -; Genomic_DNA.
DR   RefSeq; WP_012457310.1; NZ_FUFB01000007.1.
DR   AlphaFoldDB; O32389; -.
DR   SMR; O32389; -.
DR   GeneID; 29255429; -.
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..24
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   PROPEP          25..50
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000436741"
FT   CHAIN           51..670
FT                   /note="Major fimbrium tip subunit FimD"
FT                   /id="PRO_0000436742"
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