FIMA_PORGI
ID FIMA_PORGI Reviewed; 388 AA.
AC P59914;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Major fimbrium subunit FimA type-4 {ECO:0000305};
DE AltName: Full=Fimbrillin;
DE Short=Fimbrilin;
DE AltName: Full=Major fimbrial subunit protein type-4;
DE Short=FimA4 {ECO:0000303|PubMed:27062925};
DE Flags: Precursor;
GN Name=fimA; OrderedLocusNames=PG_2132;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
RN [2]
RP IDENTIFICATION, CLASSIFICATION INTO TYPE 4, AND MISCELLANEOUS.
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000303|PubMed:23809984};
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 [3] {ECO:0007744|PDB:4Q98}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 21-388, SUBCELLULAR LOCATION,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF TRP-379; 380-VAL--TRP-388 AND
RP 386-ALA--TRP-388.
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000303|PubMed:27062925};
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 (PubMed:27062925).
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. Fimbriae and their
CC constituents are major virulence factors. FimA proteins from different
CC strains have highly divergent sequences, and this has been used for
CC classification. The sequence-based classification correlates with
CC pathogenicity. {ECO:0000250|UniProtKB:B2RH54,
CC ECO:0000269|PubMed:27062925}.
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 (Probable). Linear, head-to-tail oligomerization of FimA is
CC mediated by a conformation change, facilitating the insertion of a C-
CC terminal beta-strand into a groove in the N-terminal domain of the
CC following subunit (PubMed:27062925). The anchoring subunit FimB limits
CC fimbrium length and is important for solid fimbrium attachment to the
CC outer membrane. In its absence, the major fimbriae become very long and
CC are easily detached from the membrane (PubMed:27062925).
CC {ECO:0000250|UniProtKB:B2RH54, ECO:0000269|PubMed:27062925,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:27062925}. 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 precursor. Efficient export to the
CC outer membrane and integration into fimbriae requires lipidation and
CC subsequent proteolytic removal of the lipidated propeptide.
CC {ECO:0000250|UniProtKB:B2RH54}.
CC -!- MISCELLANEOUS: Strain ATCC BAA-308 / W83 seems to lack fimbriae,
CC probably due to very low expression of the fimA gene.
CC {ECO:0000305|PubMed:23809984}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015924; AAQ67087.1; -; Genomic_DNA.
DR RefSeq; WP_005873481.1; NC_002950.2.
DR PDB; 4Q98; X-ray; 1.30 A; A=21-388.
DR PDBsum; 4Q98; -.
DR AlphaFoldDB; P59914; -.
DR SMR; P59914; -.
DR STRING; 242619.PG_2132; -.
DR PRIDE; P59914; -.
DR EnsemblBacteria; AAQ67087; AAQ67087; PG_2132.
DR KEGG; pgi:PG_2132; -.
DR HOGENOM; CLU_059924_0_0_10; -.
DR OrthoDB; 1677676at2; -.
DR Proteomes; UP000000588; Chromosome.
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:InterPro.
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 outer membrane; Fimbrium; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal; Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 19..45
FT /evidence="ECO:0000250|UniProtKB:B2RH54"
FT /id="PRO_0000009154"
FT CHAIN 46..388
FT /note="Major fimbrium subunit FimA type-4"
FT /id="PRO_0000009155"
FT REGION 379..388
FT /note="Important for oligomerization and fimbrium assembly"
FT /evidence="ECO:0000269|PubMed:27062925"
FT SITE 45..46
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 MUTAGEN 379
FT /note="W->A: Impairs oligomerization and fimbrium
FT assembly."
FT /evidence="ECO:0000269|PubMed:27062925"
FT MUTAGEN 380..388
FT /note="Missing: Abolishes fimbrium assembly."
FT /evidence="ECO:0000269|PubMed:27062925"
FT MUTAGEN 386..388
FT /note="Missing: Abolishes fimbrium assembly."
FT /evidence="ECO:0000269|PubMed:27062925"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 92..102
FT /evidence="ECO:0007829|PDB:4Q98"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4Q98"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:4Q98"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4Q98"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:4Q98"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 202..218
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:4Q98"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:4Q98"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 344..352
FT /evidence="ECO:0007829|PDB:4Q98"
FT STRAND 369..378
FT /evidence="ECO:0007829|PDB:4Q98"
SQ SEQUENCE 388 AA; 41246 MW; A9B45CA7D2142960 CRC64;
MKKTKFFLLG LAALAMTACN KDNEAEPVVE TNATVSFIIK SGESRAVGDD LTDAKITKLT
AMVYAGQVQE GIKTVEEDGG VLKVEGIPCK SGANRVLVVV ANHNYELTGK SLNEVEALTT
SLTAENQNAK NLIMTGKSAA FTIKPGSNHY GYPGGTASDN LVSAGTPLAV TRVHAGISFA
GVEVNMATQY QNYYSFKPAD AKIAALVAKK DSKIFGNSLV SNTNAYLYGV QTPAGLYTPD
AAGETYELEA SLNTNYAVGA GFYVLESKYD ASNELRPTIL CIYGKLLDKD GNPLTEPALT
DAINAGFCDG DGTTYYPVLV NYDGNGYIYS GAITQGQNKI VRNNHYKISL NITGPGTNTP
ENPQPVQANL NVTCQVTPWV VVNQAATW
