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Major fimbrium subunit FimA type-1 (Fimbrillin) (Fimbrilin) (Major fimbrial subunit protein type I)

 FIMA1_PORG3             Reviewed;         383 AA.
B2RH54; P13793; Q51821;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
06-JUL-2016, sequence version 3.
22-NOV-2017, entry version 56.
RecName: Full=Major fimbrium subunit FimA type-1;
AltName: Full=Fimbrillin;
Short=Fimbrilin {ECO:0000303|PubMed:7902712};
AltName: Full=Major fimbrial subunit protein type I;
Flags: Precursor;
Name=fimA; OrderedLocusNames=PGN_0180;
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 /
JCM 12257 / NCTC 11834 / 2561).
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
Porphyromonadaceae; Porphyromonas.
NCBI_TaxID=431947;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7902712; DOI=10.1006/bbrc.1993.2467;
Fujiwara T., Morishima S., Takahashi I., Hamada S.;
"Molecular cloning and sequencing of the fimbrilin gene of
Porphyromonas gingivalis strains and characterization of recombinant
proteins.";
Biochem. Biophys. Res. Commun. 197:241-247(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561;
PubMed=18524787; DOI=10.1093/dnares/dsn013;
Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
Nakayama K.;
"Determination of the genome sequence of Porphyromonas gingivalis
strain ATCC 33277 and genomic comparison with strain W83 revealed
extensive genome rearrangements in P. gingivalis.";
DNA Res. 15:215-225(2008).
[3]
PROTEIN SEQUENCE OF 47-59, PROTEOLYTIC PROCESSING, AND PROPEPTIDE.
PubMed=8778568; DOI=10.1016/S0882-4010(96)80006-4;
Onoe T., Hoover C.I., Nakayama K., Ideka T., Nakamura H.,
Yoshimura F.;
"Identification of Porphyromonas gingivalis prefimbrilin possessing a
long leader peptide: possible involvement of trypsin-like protease in
fimbrilin maturation.";
Microb. Pathog. 19:351-364(1995).
[4]
PROTEIN SEQUENCE OF 47-57, PROTEOLYTIC PROCESSING, SUBCELLULAR
LOCATION, AND FUNCTION.
PubMed=9786913; DOI=10.1074/jbc.273.44.29072;
Kadowaki T., Nakayama K., Yoshimura F., Okamoto K., Abe N.,
Yamamoto K.;
"Arg-gingipain acts as a major processing enzyme for various cell
surface proteins in Porphyromonas gingivalis.";
J. Biol. Chem. 273:29072-29076(1998).
[5]
DETERMINATION OF TRANSCRIPTIONAL START SITE.
PubMed=10377095;
Xie H., Lamont R.J.;
"Promoter architecture of the Porphyromonas gingivalis fimbrillin
gene.";
Infect. Immun. 67:3227-3235(1999).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561;
PubMed=12593606; DOI=10.1902/jop.2003.74.1.119;
Umemoto T., Hamada N.;
"Characterization of biologically active cell surface components of a
periodontal pathogen. The roles of major and minor fimbriae of
Porphyromonas gingivalis.";
J. Periodontology 74:119-122(2003).
[7]
FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION OF PRECURSOR, AND
MUTAGENESIS OF MET-1; CYS-19 AND VAL-37.
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561;
PubMed=15165251; DOI=10.1111/j.1365-2958.2004.04105.x;
Shoji M., Naito M., Yukitake H., Sato K., Sakai E., Ohara N.,
Nakayama K.;
"The major structural components of two cell surface filaments of
Porphyromonas gingivalis are matured through lipoprotein precursors.";
Mol. Microbiol. 52:1513-1525(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561;
PubMed=17675496; DOI=10.4049/jimmunol.179.4.2349;
Wang M., Shakhatreh M.A., James D., Liang S., Nishiyama S.,
Yoshimura F., Demuth D.R., Hajishengallis G.;
"Fimbrial proteins of porphyromonas gingivalis mediate in vivo
virulence and exploit TLR2 and complement receptor 3 to persist in
macrophages.";
J. Immunol. 179:2349-2358(2007).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561;
PubMed=17526848; DOI=10.1099/mic.0.2006/005561-0;
Nishiyama S., Murakami Y., Nagata H., Shizukuishi S., Kawagishi I.,
Yoshimura F.;
"Involvement of minor components associated with the FimA fimbriae of
Porphyromonas gingivalis in adhesive functions.";
Microbiology 153:1916-1925(2007).
[10]
FUNCTION, MISCELLANEOUS, AND SUBCELLULAR LOCATION.
PubMed=20530728; DOI=10.1177/0022034510370089;
Nagano K., Hasegawa Y., Murakami Y., Nishiyama S., Yoshimura F.;
"FimB regulates FimA fimbriation in Porphyromonas gingivalis.";
J. Dent. Res. 89:903-908(2010).
[11]
CLASSIFICATION.
PubMed=23809984; DOI=10.1111/omi.12032;
Nagano K., Abiko Y., Yoshida Y., Yoshimura F.;
"Genetic and antigenic analyses of Porphyromonas gingivalis FimA
fimbriae.";
Mol. Oral. Microbiol. 28:392-403(2013).
[12]
FUNCTION, AND SUBUNIT.
PubMed=27062925; DOI=10.1016/j.cell.2016.03.016;
Xu Q., Shoji M., Shibata S., Naito M., Sato K., Elsliger M.A.,
Grant J.C., Axelrod H.L., Chiu H.J., Farr C.L., Jaroszewski L.,
Knuth M.W., Deacon A.M., Godzik A., Lesley S.A., Curtis M.A.,
Nakayama K., Wilson I.A.;
"A distinct type of pilus from the human microbiome.";
Cell 165:690-703(2016).
-!- FUNCTION: Structural subunit of the major fimbriae. These long,
filamentous pili are attached to the cell surface; they mediate
biofilm formation, adhesion onto host cells and onto other
bacteria that are part of the oral microbiome (PubMed:9786913,
PubMed:12593606, PubMed:15165251, PubMed:17675496,
PubMed:17526848, PubMed:20530728, PubMed:27062925). They play an
important role in the invasion of periodontal tissues
(PubMed:12593606). Fimbriae and their constituents are major
virulence factors. FimA proteins from different strains have
highly divergent sequences, and this has been used for
classification (PubMed:23809984). The sequence-based
classification correlates with pathogenicity (PubMed:17675496).
{ECO:0000269|PubMed:12593606, ECO:0000269|PubMed:15165251,
ECO:0000269|PubMed:17526848, ECO:0000269|PubMed:17675496,
ECO:0000269|PubMed:20530728, ECO:0000269|PubMed:23809984,
ECO:0000269|PubMed:27062925, ECO:0000269|PubMed:9786913}.
-!- SUBUNIT: Fimbriae are composed of a major, structural subunit
(FimA) and the minor components FimC, FimD and FimE
(PubMed:17675496, PubMed:17526848). Head-to-tail oligomerization
of FimA molecules mediates assembly of the fimbrium stalk, while
the minor components probably form the fimbrium tip. Linear, head-
to-tail oligomerization of FimA is mediated by a conformation
change, facilitating the insertion of a C-terminal beta-strand
into a groove in the N-terminal domain of the following subunit
(By similarity). The anchoring subunit FimB limits fimbrium length
and is important for solid fimbrium attachment to the outer
membrane. In its absence, the major fimbriae become very long and
are easily detached from the membrane (PubMed:27062925).
{ECO:0000250|UniProtKB:P59914, ECO:0000269|PubMed:17526848,
ECO:0000269|PubMed:17675496, ECO:0000269|PubMed:27062925}.
-!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:15165251,
ECO:0000269|PubMed:17526848, ECO:0000269|PubMed:17675496,
ECO:0000269|PubMed:20530728, ECO:0000269|PubMed:9786913}. Cell
outer membrane {ECO:0000269|PubMed:15165251}. Note=Synthesized as
palmitoylated precursor. The lipidated propeptide is removed
during processing to the mature protein.
{ECO:0000269|PubMed:15165251}.
-!- PTM: Synthesized as palmitoylated precursor (PubMed:15165251).
Efficient export to the outer membrane and integration into
fimbriae requires lipidation and subsequent proteolytic removal of
the lipidated propeptide (PubMed:8778568, PubMed:9786913,
PubMed:15165251). {ECO:0000269|PubMed:15165251,
ECO:0000269|PubMed:8778568, ECO:0000269|PubMed:9786913}.
-!- DISRUPTION PHENOTYPE: FimA-deficient cells lack major fimbriae,
resulting in strongly decreased adherence to host cells
(PubMed:12593606, PubMed:17675496). Double mutants lacking both
FimA and Mfa1 lack major and minor fimbriae; they fail to adhere
to host cells. {ECO:0000269|PubMed:12593606,
ECO:0000269|PubMed:17675496}.
-!- MISCELLANEOUS: In some prokaryotes, a valine codon can be used as
start of translation. The Val-37 codon had been proposed to serve
as start of translation for FimA, but mutagenesis of Val-37 to Ala
has no effect on FimA biosynthesis. {ECO:0000269|PubMed:15165251}.
-!- MISCELLANEOUS: The name (major fimbrium subunit) does not indicate
the abundance of the protein, but is derived from the greater
length of the major fimbriae. In strain ATCC 33277 and strain ATCC
BAA-1703 / FDC 381, major fimbriae are 300 - 1600 nM in length and
about 5 nm in diameter. In contrast, minor fimbriae are only about
80 - 120 nm long. This length difference is observed only in a
small number of strains, including strain ATCC 33277 and strain
ATCC BAA-1703 / FDC 381, and is due to a loss of function mutation
in FimB, a protein that restricts fimbrial length in other
strains. {ECO:0000269|PubMed:27062925,
ECO:0000305|PubMed:20530728}.
-!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
FimA/Mfa1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA04621.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=A loosening of habits
- Issue 182 of August 2016;
URL="https://web.expasy.org/spotlight/back_issues/182/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; D17795; BAA04621.1; ALT_INIT; Genomic_DNA.
EMBL; AP009380; BAG32699.1; -; Genomic_DNA.
PIR; A27736; A27736.
RefSeq; WP_012457306.1; NC_010729.1.
SMR; B2RH54; -.
STRING; 431947.PGN_0180; -.
EnsemblBacteria; BAG32699; BAG32699; PGN_0180.
GeneID; 29255426; -.
KEGG; pgn:PGN_0180; -.
eggNOG; ENOG41077SQ; Bacteria.
eggNOG; ENOG410Z8K8; LUCA.
HOGENOM; HOG000040503; -.
OMA; CNKDNEA; -.
Proteomes; UP000008842; Chromosome.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0009289; C:pilus; IDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
InterPro; IPR029140; FimA_C.
InterPro; IPR029141; FimA_N.
InterPro; IPR008110; Fimbrillin.
Pfam; PF15495; Fimbrillin_C; 1.
Pfam; PF06321; P_gingi_FimA; 1.
PRINTS; PR01737; FIMBRILLIN.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
Cell adhesion; Cell outer membrane; Complete proteome;
Direct protein sequencing; Fimbrium; Lipoprotein; Membrane; Palmitate;
Signal; Virulence.
SIGNAL 1 18 {ECO:0000255|PROSITE-ProRule:PRU00303}.
PROPEP 19 46 {ECO:0000269|PubMed:8778568,
ECO:0000269|PubMed:9786913}.
/FTId=PRO_0000370697.
CHAIN 47 383 Major fimbrium subunit FimA type-1.
/FTId=PRO_0000370698.
REGION 374 383 Important for oligomerization and
fimbrium assembly.
{ECO:0000250|UniProtKB:P59914}.
SITE 46 47 Cleavage; by gingipain.
{ECO:0000269|PubMed:15165251,
ECO:0000269|PubMed:9786913}.
LIPID 19 19 N-palmitoyl cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303,
ECO:0000305|PubMed:15165251}.
LIPID 19 19 S-diacylglycerol cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303,
ECO:0000305|PubMed:15165251}.
MUTAGEN 1 1 M->A: Abolishes FimA biosynthesis.
{ECO:0000269|PubMed:15165251}.
MUTAGEN 19 19 C->A: Impairs cleavage by lipoprotein
signal peptidase and subsequent
processing steps.
{ECO:0000269|PubMed:15165251}.
MUTAGEN 37 37 V->A: No effect.
{ECO:0000269|PubMed:15165251}.
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


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