FIMA7_PORGN
ID FIMA7_PORGN Reviewed; 386 AA.
AC Q51825;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Major fimbrium subunit FimA type-2;
DE AltName: Full=Fimbrillin;
DE Short=Fimbrilin;
DE AltName: Full=Major fimbrial subunit protein type II;
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 49417 / RB22 D-1;
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 FUNCTION, SUBCELLULAR LOCATION, AND 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 (Probable). These
CC long, filamentous pili are attached to the cell surface; they mediate
CC biofilm formation, adhesion onto host cells and onto other bacteria
CC that are part of the oral microbiome. They play an important role in
CC the invasion of periodontal tissues. 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 The sequence-based classification correlates with pathogenicity.
CC {ECO:0000250|UniProtKB:B2RH54, ECO:0000269|PubMed:23809984,
CC 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:23809984}. 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 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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC FimA/Mfa1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA04626.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D17800; BAA04626.1; ALT_INIT; Genomic_DNA.
DR PIR; D60275; D60275.
DR PIR; JN0919; JN0919.
DR AlphaFoldDB; Q51825; -.
DR SMR; Q51825; -.
DR PRIDE; Q51825; -.
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_0000009162"
FT CHAIN 47..386
FT /note="Major fimbrium subunit FimA type-2"
FT /id="PRO_0000009163"
FT REGION 377..386
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 386 AA; 41691 MW; 80AA1665EFC5898A CRC64;
MKKTKFFLLG LAALAMTACN KDNEAEPVTE GNATISVVLK TSNPNRAFGN AGDEAKVAKL
TVMVYKGEQQ EAIKSAENAT KVENIKCSAG QRTLVVMANT GGMELAGKTL AEVKALTTEL
TEGNQEAAGL IMTAEPVEVT LVAGNNYYGY DGSQGGNQIS QDTPLEIKRV RARIAFTKIE
VTMSQSYANK YNFAPENIYA LVAKKKSNLF GASLANNDDA YLTGSLTTFN GAYTPANYTH
VDWLGRDFTE PSNNAPQGFY VLESTYAQNA GLRPTILCIK GKLTKHDGTP LSSEEMTAAF
NAGWIVANND PTTYYPVLVN FESNNYTYTG EAVEKGKIVR NHKFDINLTI TGPGTNNPEN
PITESANLNV NCVVAAWKGV VQNVIW
