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 27-MAR-2024, entry version 54.
DE RecName: Full=Major fimbrium tip subunit FimD;
DE Flags: Precursor;
GN Name=fimD {ECO:0000312|EMBL:BAA22417.1};
OS Porphyromonas gingivalis.
OC Bacteria; Bacteroidota; 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}.
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; D42067; BAA22417.1; -; Genomic_DNA.
DR RefSeq; WP_012457310.1; NZ_JAVIVL010000003.1.
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 Gene3D; 2.60.40.3690; -; 1.
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
//
