FIMA6_PORGN
ID FIMA6_PORGN Reviewed; 383 AA.
AC Q93R80;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 2.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Major fimbrium subunit FimA type Ib;
DE AltName: Full=Fimbrillin;
DE Short=Fimbrilin;
DE Flags: Precursor;
GN Name=fimA;
OS Porphyromonas gingivalis.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=837;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HG1691;
RA Nakagawa I., Amano A., Ohara-Nemoto T., Endoh N., Morisaki I., Kimura S.,
RA Hamada S.;
RT "Identification of a new fimA gene of Porphyromonas gingivalis and its
RT distribution in Janapanese adult and disables population with
RT periodontitis.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Structural subunit of the major fimbriae. 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 the
CC invasion of periodontal tissues. Fimbriae and their constituents are
CC major virulence factors. FimA proteins from different strains have
CC highly divergent sequences, and this has been used for classification.
CC The sequence-based classification correlates with pathogenicity.
CC {ECO:0000250|UniProtKB:B2RH54}.
CC -!- SUBUNIT: Fimbriae are composed of a major, structural subunit (FimA)
CC and the minor components FimC, FimD and FimE (By similarity). Head-to-
CC tail oligomerization of FimA molecules mediates assembly of the
CC fimbrium stalk, while the minor components probably form the fimbrium
CC tip. Linear, head-to-tail oligomerization of FimA is mediated by a
CC conformation change, facilitating the insertion of a C-terminal beta-
CC strand into a groove in the N-terminal domain of the following subunit
CC (By similarity). {ECO:0000250|UniProtKB:B2RH54,
CC ECO:0000250|UniProtKB:P59914}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250|UniProtKB:B2RH54}. Cell
CC outer membrane {ECO:0000250|UniProtKB:B2RH54}. Note=Synthesized as
CC palmitoylated precursor. The lipidated propeptide is removed during
CC processing to the mature protein. {ECO:0000250|UniProtKB:B2RH54}.
CC -!- PTM: Synthesized as palmitoylated lipoprotein precursor. Efficient
CC export to the outer membrane and integration into fimbriae requires
CC lipidation and subsequent proteolytic removal of the lipidated
CC propeptide. {ECO:0000250|UniProtKB:B2RH54}.
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 bacteroidetes fimbrillin superfamily.
CC FimA/Mfa1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB61734.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB058848; BAB61734.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q93R80; -.
DR SMR; Q93R80; -.
DR PRIDE; Q93R80; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR029141; FimA_N.
DR InterPro; IPR008110; Fimbrillin.
DR Pfam; PF06321; P_gingi_FimA; 1.
DR PRINTS; PR01737; FIMBRILLIN.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell adhesion; Cell outer membrane; Fimbrium; Lipoprotein; Membrane;
KW Palmitate; Signal; Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 19..46
FT /evidence="ECO:0000250|UniProtKB:B2RH54"
FT /id="PRO_0000009158"
FT CHAIN 47..383
FT /note="Major fimbrium subunit FimA type Ib"
FT /id="PRO_0000009159"
FT REGION 374..383
FT /note="Important for oligomerization and fimbrium assembly"
FT /evidence="ECO:0000250|UniProtKB:P59914"
FT SITE 46..47
FT /note="Cleavage; by gingipain"
FT /evidence="ECO:0000250|UniProtKB:B2RH54"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 383 AA; 41457 MW; 88F19F0EDBC6812B CRC64;
MKKTKFFLLG LAALAMTACN KDNEAEPVTE GNATISVVLK TSNSNRAFGV GDDESKVAKL
TVMVYNGEQQ EAIKSAENAT KVEDIKCSAG QRTLVVMANT GAMELVGKTL AEVKALTTEL
TAENQEAAGL IMTAEPKTIV LKAGKNYIGY SGTGEGNHIE NDPLKIKRVH ARMAFTEIKV
QMSAAYDNIY TFVPEKIYGL IAKKQSNLFG ATLVNADANY LTGSLTTFNG AYTPANYANV
PWLSRDYIAP TADAPQGFYV LENDYSANSG TIHPTILCVY GKLQKNGADL TGTDLAAAQA
ANWVDGQGKT YYPVLVNFNS NNYTYDNGYT PKNKIERNHK YDIKLTITGP GTNNPENPIT
ESAHLNVQCT VAEWVLVGQN ATW
