MFA1_PORG3
ID MFA1_PORG3 Reviewed; 563 AA.
AC B2RHG1;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Minor fimbrium subunit Mfa1 {ECO:0000303|PubMed:19589838};
DE AltName: Full=Pg-II fim a {ECO:0000303|PubMed:19589838};
DE Flags: Precursor;
GN Name=mfa1 {ECO:0000312|EMBL:BAG32806.1};
GN OrderedLocusNames=PGN_0287 {ECO:0000312|EMBL:BAG32806.1};
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] {ECO:0000312|EMBL:BAG32806.1, ECO:0000312|Proteomes:UP000008842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000312|Proteomes:UP000008842};
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 [2]
RP PROTEIN SEQUENCE OF 50-60, PROTEOLYTIC PROCESSING, AND SUBCELLULAR
RP LOCATION.
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 [3]
RP PROTEIN SEQUENCE OF 460-475, FUNCTION, INTERACTION WITH S.GORDONII SSP5,
RP AND SUBCELLULAR LOCATION.
RX PubMed=11083792; DOI=10.1128/iai.68.12.6758-6762.2000;
RA Chung W.O., Demuth D.R., Lamont R.J.;
RT "Identification of a Porphyromonas gingivalis receptor for the
RT Streptococcus gordonii SspB protein.";
RL Infect. Immun. 68:6758-6762(2000).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:12593606};
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 [5]
RP FUNCTION, INTERACTION WITH S.GORDONII SSP5, AND SUBCELLULAR LOCATION.
RX PubMed=15972485; DOI=10.1128/iai.73.7.3983-3989.2005;
RA Park Y., Simionato M.R., Sekiya K., Murakami Y., James D., Chen W.,
RA Hackett M., Yoshimura F., Demuth D.R., Lamont R.J.;
RT "Short fimbriae of Porphyromonas gingivalis and their role in coadhesion
RT with Streptococcus gordonii.";
RL Infect. Immun. 73:3983-3989(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH MFA2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:19589838};
RX PubMed=19589838; DOI=10.1099/mic.0.028928-0;
RA Hasegawa Y., Iwami J., Sato K., Park Y., Nishikawa K., Atsumi T.,
RA Moriguchi K., Murakami Y., Lamont R.J., Nakamura H., Ohno N., Yoshimura F.;
RT "Anchoring and length regulation of Porphyromonas gingivalis Mfa1 fimbriae
RT by the downstream gene product Mfa2.";
RL Microbiology 155:3333-3347(2009).
RN [7]
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).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:24118823};
RX PubMed=24118823; DOI=10.1111/omi.12040;
RA Hasegawa Y., Nagano K., Ikai R., Izumigawa M., Yoshida Y., Kitai N.,
RA Lamont R.J., Murakami Y., Yoshimura F.;
RT "Localization and function of the accessory protein Mfa3 in Porphyromonas
RT gingivalis Mfa1 fimbriae.";
RL Mol. Oral. Microbiol. 28:467-480(2013).
RN [9]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:26001707};
RX PubMed=26001707; DOI=10.1177/0022034515588275;
RA Nagano K., Hasegawa Y., Yoshida Y., Yoshimura F.;
RT "A major fimbrilin variant of Mfa1 fimbriae in Porphyromonas gingivalis.";
RL J. Dent. Res. 94:1143-1148(2015).
RN [10]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:26437277};
RX PubMed=26437277; DOI=10.1371/journal.pone.0139454;
RA Ikai R., Hasegawa Y., Izumigawa M., Nagano K., Yoshida Y., Kitai N.,
RA Lamont R.J., Yoshimura F., Murakami Y.;
RT "Mfa4, an accessory protein of Mfa1 fimbriae, modulates fimbrial
RT biogenesis, cell auto-aggregation, and biofilm formation in Porphyromonas
RT gingivalis.";
RL PLoS ONE 10:E0139454-E0139454(2015).
CC -!- FUNCTION: Structural subunit of the minor fimbriae (PubMed:12593606,
CC PubMed:19589838, PubMed:24118823). These filamentous pili are attached
CC to the cell surface; they mediate biofilm formation, adhesion onto host
CC cells and onto other bacteria that are part of the oral microbiome
CC (PubMed:11083792, PubMed:12593606, PubMed:15972485, PubMed:19589838,
CC PubMed:23809984, PubMed:24118823, PubMed:26001707, PubMed:26437277).
CC They play an important role in invasion of periodontal tissues and are
CC recognized as major virulence factors. Mfa1 orthologs from different
CC strains have highly divergent sequences, and this correlates with
CC pathogenicity (Probable). {ECO:0000269|PubMed:11083792,
CC ECO:0000269|PubMed:12593606, ECO:0000269|PubMed:15972485,
CC ECO:0000269|PubMed:19589838, ECO:0000269|PubMed:23809984,
CC ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707,
CC ECO:0000269|PubMed:26437277, ECO:0000305}.
CC -!- SUBUNIT: Structural component of the fimbrial stalk. Minor fimbriae are
CC composed of a structural subunit, most often Mfa1, and the accessory
CC subunits Mfa3, Mfa4 and Mfa5 (PubMed:19589838, PubMed:24118823,
CC PubMed:26001707, PubMed:26437277). Mfa1 interacts with Mfa2; this
CC anchors the fimbrium in the membrane (PubMed:19589838). Fimbrium
CC assembly occurs by linear, head-to-tail oligomerization of fimbrial
CC subunits. This is mediated via insertion of a C-terminal beta-strand
CC from one subunit into a groove in the N-terminal domain of the
CC following subunit (Probable). Interacts with S.gordonii ssp5
CC (PubMed:11083792, PubMed:15972485). {ECO:0000269|PubMed:11083792,
CC ECO:0000269|PubMed:15972485, ECO:0000269|PubMed:19589838,
CC ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707,
CC ECO:0000269|PubMed:26437277, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:19589838,
CC ECO:0000269|PubMed:23809984, ECO:0000269|PubMed:24118823,
CC ECO:0000269|PubMed:26001707, ECO:0000269|PubMed:26437277}. Cell outer
CC membrane {ECO:0000269|PubMed:11083792, ECO:0000269|PubMed:15972485,
CC ECO:0000305|PubMed:9786913}. Note=Probably synthesized as a
CC palmitoylated precursor. Efficient export to the outer membrane and
CC integration into fimbriae requires lipidation and subsequent
CC proteolytic removal of the lipidated propeptide (Probable).
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mfa1-deficient cells show increased
CC autoaggregation. Double mutants lacking both FimA and Mfa1 lack major
CC and minor fimbriae; they fail to adhere to host cells.
CC {ECO:0000269|PubMed:12593606}.
CC -!- MISCELLANEOUS: The name (minor 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:0000305}.
CC -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC {ECO:0000305}.
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DR EMBL; AP009380; BAG32806.1; -; Genomic_DNA.
DR RefSeq; WP_012457396.1; NZ_CP025930.1.
DR PDB; 5NF2; X-ray; 1.73 A; A=65-563.
DR PDB; 5NF3; X-ray; 1.97 A; A=32-554.
DR PDBsum; 5NF2; -.
DR PDBsum; 5NF3; -.
DR AlphaFoldDB; B2RHG1; -.
DR SMR; B2RHG1; -.
DR STRING; 431947.PGN_0287; -.
DR PRIDE; B2RHG1; -.
DR EnsemblBacteria; BAG32806; BAG32806; PGN_0287.
DR GeneID; 29255533; -.
DR KEGG; pgn:PGN_0287; -.
DR eggNOG; ENOG50339MN; Bacteria.
DR HOGENOM; CLU_492390_0_0_10; -.
DR OMA; HTNATEY; -.
DR BioCyc; PGIN431947:G1G2V-314-MON; -.
DR Proteomes; UP000008842; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019867; C:outer membrane; IDA:UniProtKB.
DR GO; GO:0009418; C:pilus shaft; IMP:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
DR InterPro; IPR029140; FimA_C.
DR Pfam; PF15495; Fimbrillin_C; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing; Fimbrium;
KW Lipoprotein; Membrane; Palmitate; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 20..49
FT /evidence="ECO:0000269|PubMed:9786913"
FT /id="PRO_0000436790"
FT CHAIN 50..563
FT /note="Minor fimbrium subunit Mfa1"
FT /id="PRO_0000436791"
FT REGION 504..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 49..50
FT /note="Cleavage; by gingipain"
FT /evidence="ECO:0000269|PubMed:9786913"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:5NF3"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5NF2"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:5NF2"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:5NF2"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:5NF3"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:5NF3"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 265..278
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5NF2"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:5NF2"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:5NF2"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 388..397
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:5NF2"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 436..439
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:5NF2"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 459..467
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 486..494
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 544..552
FT /evidence="ECO:0007829|PDB:5NF2"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:5NF2"
SQ SEQUENCE 563 AA; 60786 MW; 65F205CBDFF5A173 CRC64;
MKLNKMFLVG ALLSLGFASC SKEGNGPDPD NAAKSYMSMT LSMPMGSARA GDGQDQANPD
YHYVGEWAGK DKIEKVSIYM VPQGGPGLVE SAEDLDFGTY YENPTIDPAT HNAILKPKKG
IKVNSAVGKT VKVYVVLNDI AGKAKALLAN VNAADFDAKF KEIIELSTQA QALGTVADGP
NPATAAGKIA KKNGTTDETI MMTCLQPSDA LTIEAAVSEA NAIAGIKNQA KVTVERSVAR
AMVSTKAQSY EIKATTQIGE IAAGSVLATI TDIRWVVAQG ERRQYLSKKR GTVPENTWVT
PGSGFVPTSS TFHTNATEYY DYAGLWEDHN TNEAVISGTQ VPTLADYQLQ DVTGELANAL
SGKFLLPNTH KSGANAASSD YKRGNTAYVL VRAKFTPKKE AFIDRGKTYS DNTAVPEYVA
GEDFFVGENG QFYVSMKSVT DPKVGGVAGM KAHKYVKGKV LYYAWLNPST TSPDSWWNSP
VVRNNIYHIH IKSIKKLGFN WNPLVPDPDP SNPENPNNPD PNPDEPGTPV PTDPENPLPD
QDTFMSVEVT VLPWKVHSYE VDL
