FIMA1_PORG3
ID FIMA1_PORG3 Reviewed; 383 AA.
AC B2RH54; P13793; Q51821;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 3.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Major fimbrium subunit FimA type-1;
DE AltName: Full=Fimbrillin;
DE Short=Fimbrilin {ECO:0000303|PubMed:7902712};
DE AltName: Full=Major fimbrial subunit protein type I;
DE Flags: Precursor;
GN Name=fimA; OrderedLocusNames=PGN_0180;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7902712; DOI=10.1006/bbrc.1993.2467;
RA Fujiwara T., Morishima S., Takahashi I., Hamada S.;
RT "Molecular cloning and sequencing of the fimbrilin gene of Porphyromonas
RT gingivalis strains and characterization of recombinant proteins.";
RL Biochem. Biophys. Res. Commun. 197:241-247(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
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 [3]
RP PROTEIN SEQUENCE OF 47-59, PROTEOLYTIC PROCESSING, AND PROPEPTIDE.
RX PubMed=8778568; DOI=10.1016/s0882-4010(96)80006-4;
RA Onoe T., Hoover C.I., Nakayama K., Ideka T., Nakamura H., Yoshimura F.;
RT "Identification of Porphyromonas gingivalis prefimbrilin possessing a long
RT leader peptide: possible involvement of trypsin-like protease in fimbrilin
RT maturation.";
RL Microb. Pathog. 19:351-364(1995).
RN [4]
RP PROTEIN SEQUENCE OF 47-57, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RX PubMed=9786913; DOI=10.1074/jbc.273.44.29072;
RA Kadowaki T., Nakayama K., Yoshimura F., Okamoto K., Abe N., Yamamoto K.;
RT "Arg-gingipain acts as a major processing enzyme for various cell surface
RT proteins in Porphyromonas gingivalis.";
RL J. Biol. Chem. 273:29072-29076(1998).
RN [5]
RP DETERMINATION OF TRANSCRIPTIONAL START SITE.
RX PubMed=10377095; DOI=10.1128/iai.67.7.3227-3235.1999;
RA Xie H., Lamont R.J.;
RT "Promoter architecture of the Porphyromonas gingivalis fimbrillin gene.";
RL Infect. Immun. 67:3227-3235(1999).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=12593606; DOI=10.1902/jop.2003.74.1.119;
RA Umemoto T., Hamada N.;
RT "Characterization of biologically active cell surface components of a
RT periodontal pathogen. The roles of major and minor fimbriae of
RT Porphyromonas gingivalis.";
RL J. Periodontology 74:119-122(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-19 OF PRECURSOR,
RP DIACYLGLYCEROL AT CYS-19 OF PRECURSOR, AND MUTAGENESIS OF MET-1; CYS-19 AND
RP VAL-37.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=15165251; DOI=10.1111/j.1365-2958.2004.04105.x;
RA Shoji M., Naito M., Yukitake H., Sato K., Sakai E., Ohara N., Nakayama K.;
RT "The major structural components of two cell surface filaments of
RT Porphyromonas gingivalis are matured through lipoprotein precursors.";
RL Mol. Microbiol. 52:1513-1525(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
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 [10]
RP FUNCTION, MISCELLANEOUS, AND SUBCELLULAR LOCATION.
RX PubMed=20530728; DOI=10.1177/0022034510370089;
RA Nagano K., Hasegawa Y., Murakami Y., Nishiyama S., Yoshimura F.;
RT "FimB regulates FimA fimbriation in Porphyromonas gingivalis.";
RL J. Dent. Res. 89:903-908(2010).
RN [11]
RP CLASSIFICATION.
RX PubMed=23809984; DOI=10.1111/omi.12032;
RA Nagano K., Abiko Y., Yoshida Y., Yoshimura F.;
RT "Genetic and antigenic analyses of Porphyromonas gingivalis FimA
RT fimbriae.";
RL Mol. Oral. Microbiol. 28:392-403(2013).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=27062925; DOI=10.1016/j.cell.2016.03.016;
RA Xu Q., Shoji M., Shibata S., Naito M., Sato K., Elsliger M.A., Grant J.C.,
RA Axelrod H.L., Chiu H.J., Farr C.L., Jaroszewski L., Knuth M.W.,
RA Deacon A.M., Godzik A., Lesley S.A., Curtis M.A., Nakayama K., Wilson I.A.;
RT "A distinct type of pilus from the human microbiome.";
RL Cell 165:690-703(2016).
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 (PubMed:9786913, PubMed:12593606,
CC PubMed:15165251, PubMed:17675496, PubMed:17526848, PubMed:20530728,
CC PubMed:27062925). They play an important role in the invasion of
CC periodontal tissues (PubMed:12593606). Fimbriae and their constituents
CC are major virulence factors. FimA proteins from different strains have
CC highly divergent sequences, and this has been used for classification
CC (PubMed:23809984). The sequence-based classification correlates with
CC pathogenicity (PubMed:17675496). {ECO:0000269|PubMed:12593606,
CC ECO:0000269|PubMed:15165251, ECO:0000269|PubMed:17526848,
CC ECO:0000269|PubMed:17675496, ECO:0000269|PubMed:20530728,
CC ECO:0000269|PubMed:23809984, ECO:0000269|PubMed:27062925,
CC ECO:0000269|PubMed:9786913}.
CC -!- SUBUNIT: Fimbriae are composed of a major, structural subunit (FimA)
CC and the minor components FimC, FimD and FimE (PubMed:17675496,
CC PubMed:17526848). Head-to-tail oligomerization of FimA molecules
CC mediates assembly of the fimbrium stalk, while the minor components
CC probably form the fimbrium tip. Linear, head-to-tail oligomerization of
CC FimA is mediated by a conformation change, facilitating the insertion
CC of a C-terminal beta-strand into a groove in the N-terminal domain of
CC the following subunit (By similarity). The anchoring subunit FimB
CC limits fimbrium length and is important for solid fimbrium attachment
CC to the outer membrane. In its absence, the major fimbriae become very
CC long and are easily detached from the membrane (PubMed:27062925).
CC {ECO:0000250|UniProtKB:P59914, ECO:0000269|PubMed:17526848,
CC ECO:0000269|PubMed:17675496, ECO:0000269|PubMed:27062925}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:15165251,
CC ECO:0000269|PubMed:17526848, ECO:0000269|PubMed:17675496,
CC ECO:0000269|PubMed:20530728, ECO:0000269|PubMed:9786913}. Cell outer
CC membrane {ECO:0000269|PubMed:15165251}. Note=Synthesized as
CC palmitoylated precursor. The lipidated propeptide is removed during
CC processing to the mature protein. {ECO:0000269|PubMed:15165251}.
CC -!- PTM: Synthesized as palmitoylated precursor (PubMed:15165251).
CC Efficient export to the outer membrane and integration into fimbriae
CC requires lipidation and subsequent proteolytic removal of the lipidated
CC propeptide (PubMed:8778568, PubMed:9786913, PubMed:15165251).
CC {ECO:0000269|PubMed:15165251, ECO:0000269|PubMed:8778568,
CC ECO:0000269|PubMed:9786913}.
CC -!- DISRUPTION PHENOTYPE: FimA-deficient cells lack major fimbriae,
CC resulting in strongly decreased adherence to host cells
CC (PubMed:12593606, PubMed:17675496). Double mutants lacking both FimA
CC and Mfa1 lack major and minor fimbriae; they fail to adhere to host
CC cells. {ECO:0000269|PubMed:12593606, ECO:0000269|PubMed:17675496}.
CC -!- MISCELLANEOUS: In some prokaryotes, a valine codon can be used as start
CC of translation. The Val-37 codon had been proposed to serve as start of
CC translation for FimA, but mutagenesis of Val-37 to Ala has no effect on
CC FimA biosynthesis. {ECO:0000269|PubMed:15165251}.
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:0000269|PubMed:27062925,
CC ECO:0000305|PubMed:20530728}.
CC -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC FimA/Mfa1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA04621.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; D17795; BAA04621.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP009380; BAG32699.1; -; Genomic_DNA.
DR PIR; A27736; A27736.
DR RefSeq; WP_012457306.1; NZ_CP025930.1.
DR PDB; 6JZK; X-ray; 2.10 A; A/B=20-383.
DR PDB; 6KMF; EM; 3.60 A; A/B/C/D=47-383.
DR PDBsum; 6JZK; -.
DR PDBsum; 6KMF; -.
DR AlphaFoldDB; B2RH54; -.
DR SMR; B2RH54; -.
DR STRING; 431947.PGN_0180; -.
DR ABCD; B2RH54; 2 sequenced antibodies.
DR EnsemblBacteria; BAG32699; BAG32699; PGN_0180.
DR GeneID; 29255426; -.
DR KEGG; pgn:PGN_0180; -.
DR eggNOG; ENOG5033GET; Bacteria.
DR HOGENOM; CLU_059924_0_0_10; -.
DR OMA; CNKDNEA; -.
DR BioCyc; PGIN431947:G1G2V-197-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:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR029140; FimA_C.
DR InterPro; IPR029141; FimA_N.
DR InterPro; IPR008110; Fimbrillin.
DR Pfam; PF15495; Fimbrillin_C; 1.
DR Pfam; PF06321; P_gingi_FimA; 1.
DR PRINTS; PR01737; FIMBRILLIN.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell outer membrane;
KW Direct protein sequencing; Fimbrium; Lipoprotein; Membrane; Palmitate;
KW Signal; Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 19..46
FT /evidence="ECO:0000269|PubMed:8778568,
FT ECO:0000269|PubMed:9786913"
FT /id="PRO_0000370697"
FT CHAIN 47..383
FT /note="Major fimbrium subunit FimA type-1"
FT /id="PRO_0000370698"
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:0000269|PubMed:15165251,
FT ECO:0000269|PubMed:9786913"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000305|PubMed:15165251"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000305|PubMed:15165251"
FT MUTAGEN 1
FT /note="M->A: Abolishes FimA biosynthesis."
FT /evidence="ECO:0000269|PubMed:15165251"
FT MUTAGEN 19
FT /note="C->A: Impairs cleavage by lipoprotein signal
FT peptidase and subsequent processing steps."
FT /evidence="ECO:0000269|PubMed:15165251"
FT MUTAGEN 37
FT /note="V->A: No effect."
FT /evidence="ECO:0000269|PubMed:15165251"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:6JZK"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 80..98
FT /evidence="ECO:0007829|PDB:6JZK"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6JZK"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:6JZK"
FT TURN 184..189
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 190..203
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:6JZK"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:6JZK"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:6JZK"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 339..347
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6JZK"
FT STRAND 365..373
FT /evidence="ECO:0007829|PDB:6JZK"
SQ SEQUENCE 383 AA; 41367 MW; 5E99610BD45F69F1 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
PWLSRNYVAP AADAPQGFYV LENDYSANGG TIHPTILCVY GKLQKNGADL AGADLAAAQA
ANWVDAEGKT YYPVLVNFNS NNYTYDSNYT PKNKIERNHK YDIKLTITGP GTNNPENPIT
ESAHLNVQCT VAEWVLVGQN ATW
