FIMA1_PORGN
ID FIMA1_PORGN Reviewed; 383 AA.
AC P0C940; P13793; Q51821;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 2.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Major fimbrium subunit FimA type-1;
DE Short=FimA1;
DE AltName: Full=Fimbrillin;
DE Short=Fimbrilin;
DE AltName: Full=Major fimbrial subunit protein type I;
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=ATCC BAA-1703 / FDC 381;
RX PubMed=2895100; DOI=10.1128/jb.170.4.1658-1665.1988;
RA Dickinson D.P., Kubiniec M.A., Yoshimura F., Genco R.J.;
RT "Molecular cloning and sequencing of the gene encoding the fimbrial subunit
RT protein of Bacteroides gingivalis.";
RL J. Bacteriol. 170:1658-1665(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-1703 / FDC 381, and BH18/10;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-383.
RC STRAIN=ATCC BAA-1703 / FDC 381;
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 [4]
RP PROTEIN SEQUENCE OF 47-67, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-1703 / FDC 381;
RX PubMed=1987052; DOI=10.1128/iai.59.1.383-389.1991;
RA Lee J.Y., Sojar H.T., Bedi G.S., Genco R.J.;
RT "Porphyromonas (Bacteroides) gingivalis fimbrillin: size, amino-terminal
RT sequence, and antigenic heterogeneity.";
RL Infect. Immun. 59:383-389(1991).
RN [5]
RP FUNCTION, AND CLASSIFICATION INTO TYPES.
RX PubMed=11748193; DOI=10.1128/iai.70.1.277-285.2002;
RA Nakagawa I., Amano A., Kuboniwa M., Nakamura T., Kawabata S., Hamada S.;
RT "Functional differences among FimA variants of Porphyromonas gingivalis and
RT their effects on adhesion to and invasion of human epithelial cells.";
RL Infect. Immun. 70:277-285(2002).
RN [6]
RP MISCELLANEOUS.
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 [7]
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).
CC -!- FUNCTION: Structural subunit of the major fimbriae (PubMed:1987052).
CC These long, filamentous pili are attached to the cell surface; they
CC mediate biofilm formation, adhesion onto host cells and onto other
CC bacteria that are part of the oral microbiome. They play an important
CC role in the invasion of periodontal tissues (PubMed:1987052,
CC PubMed:11748193). Fimbriae and their constituents are major virulence
CC factors. FimA proteins from different strains have highly divergent
CC sequences, and this has been used for classification. The sequence-
CC based classification correlates with pathogenicity.
CC {ECO:0000250|UniProtKB:B2RH54, ECO:0000269|PubMed:11748193,
CC ECO:0000269|PubMed:1987052, ECO:0000305}.
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:0000269|PubMed:1987052}. Cell outer
CC 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 381, major fimbriae are
CC 300 - 1600 nM in length and about 5 nm in diameter. In contrast, minor
CC fimbriae are only about 80 - 120 nm long. This length difference is
CC observed only in a small number of strains, including strain ATCC 33277
CC and strain 381, and is due to a loss of function mutation in FimB, a
CC protein that restricts fimbrial length in other strains.
CC {ECO:0000305|PubMed:20530728}.
CC -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC FimA/Mfa1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16482.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA04620.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA04622.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M19405; AAA16482.1; ALT_INIT; Unassigned_DNA.
DR EMBL; D17794; BAA04620.1; ALT_INIT; Genomic_DNA.
DR EMBL; D17796; BAA04622.1; ALT_INIT; Genomic_DNA.
DR EMBL; D42067; BAA22414.1; -; Genomic_DNA.
DR PIR; A27736; A27736.
DR PIR; JN0915; JN0915.
DR RefSeq; WP_012457306.1; NZ_FUFB01000007.1.
DR AlphaFoldDB; P0C940; -.
DR SMR; P0C940; -.
DR PRIDE; P0C940; -.
DR GeneID; 29255426; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
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 Cell adhesion; Cell outer membrane; Direct protein sequencing; Fimbrium;
KW Lipoprotein; Membrane; Palmitate; Signal; Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 19..46
FT /evidence="ECO:0000269|PubMed:1987052"
FT /id="PRO_0000009156"
FT CHAIN 47..383
FT /note="Major fimbrium subunit FimA type-1"
FT /id="PRO_0000009157"
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"
FT VARIANT 247
FT /note="Y -> C (in strain: BH18/10)"
FT CONFLICT 164
FT /note="L -> H (in Ref. 1; AAA16482)"
FT /evidence="ECO:0000305"
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
