ID MFA3_PORG3 Reviewed; 446 AA.
AC B2RHG3;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Minor fimbrium tip subunit Mfa3;
DE Flags: Precursor;
GN Name=mfa3; OrderedLocusNames=PGN_0289 {ECO:0000312|EMBL:BAG32808.1};
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1] {ECO:0000312|EMBL:BAG32808.1, 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 IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND SUBUNIT.
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 [3]
RP PROTEIN SEQUENCE OF 44-51, SUBCELLULAR LOCATION, FUNCTION, SUBUNIT,
RP PROPEPTIDE, AND DISRUPTION PHENOTYPE.
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 [4]
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 [5]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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: Tip subunit of the minor fimbriae. These filamentous pili are
CC attached to the cell surface; they mediate biofilm formation, adhesion
CC onto host cells and onto other bacteria that are part of the oral
CC microbiome (PubMed:24118823, PubMed:26001707). They play an important
CC role in invasion of periodontal tissues and are recognized as major
CC virulence factors. Fimbrium subunits from different strains have highly
CC divergent sequences, and this correlates with pathogenicity (Probable).
CC {ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707,
CC ECO:0000305}.
CC -!- SUBUNIT: Component of the fimbrium tip (PubMed:24118823). Minor
CC fimbriae are composed of a structural subunit, most often Mfa1, and the
CC accessory subunits Mfa3, Mfa4 and Mfa5 (PubMed:19589838,
CC PubMed:24118823, PubMed:26001707). Fimbrium assembly occurs by linear,
CC head-to-tail oligomerization of fimbrial subunits. This is mediated via
CC insertion of a C-terminal beta-strand from one subunit into a groove in
CC the N-terminal domain of the following subunit (Probable). Mfa3 is
CC required for Mfa4 and Mfa5 insertion into the fimbrium
CC (PubMed:24118823). {ECO:0000269|PubMed:19589838,
CC ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:19589838,
CC ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707}. Cell outer
CC membrane {ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26437277}.
CC Note=Targeted to the outer membrane as a palmitoylated precursor. The
CC lipid modification is no longer present after proteolytic processing to
CC the mature form (PubMed:26437277). Detected at the tip of the fimbriae
CC (PubMed:24118823). {ECO:0000269|PubMed:24118823,
CC ECO:0000305|PubMed:26437277}.
CC -!- DISRUPTION PHENOTYPE: Mildly increased autoaggregation.
CC {ECO:0000269|PubMed:24118823}.
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 FimB/Mfa2 family. {ECO:0000305}.
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DR EMBL; AP009380; BAG32808.1; -; Genomic_DNA.
DR RefSeq; WP_012457397.1; NZ_CP025930.1.
DR PDB; 5NF4; X-ray; 1.75 A; A/B=23-446.
DR PDBsum; 5NF4; -.
DR AlphaFoldDB; B2RHG3; -.
DR SMR; B2RHG3; -.
DR GeneID; 29255535; -.
DR KEGG; pgn:PGN_0289; -.
DR eggNOG; ENOG502ZBHU; Bacteria.
DR HOGENOM; CLU_051995_0_0_10; -.
DR OrthoDB; 1014294at2; -.
DR BioCyc; PGIN431947:G1G2V-316-MONOMER; -.
DR Proteomes; UP000008842; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IDA:UniProtKB.
DR GO; GO:0009419; C:pilus tip; IDA:UniProtKB.
DR InterPro; IPR014941; FimB/Mfa2/Mfa3.
DR Pfam; PF08842; Mfa2; 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..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 21..43
FT /evidence="ECO:0000269|PubMed:24118823"
FT /id="PRO_0000436795"
FT CHAIN 44..446
FT /note="Minor fimbrium tip subunit Mfa3"
FT /id="PRO_5002781645"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:5NF4"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:5NF4"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:5NF4"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:5NF4"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:5NF4"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5NF4"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 183..200
FT /evidence="ECO:0007829|PDB:5NF4"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:5NF4"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:5NF4"
FT STRAND 332..340
FT /evidence="ECO:0007829|PDB:5NF4"
SQ SEQUENCE 446 AA; 50047 MW; A154AFE8FDC7972C CRC64;
MMQLKKRYFA LILLLFLWSG CDRGVDPQPD PLQPDVYLLV NARAAHTNGE ESINMDAEDF
EDRVHSLAML VFDSNTGEKV AEHFSSSIGS GTSTYVFTVK LKPGQRDFFF VANIPNMQTA
MASIVNKSDM NHFMQVFRDL DPIHYHNATN NNGFPMSRMY SNQTVTIGGT ITQPLPFKPD
GENNVKLQRV VAKLDVNIVE GVENLQKIEL CNANVHYRLV PNQSEPIQFY GPVELRRVGA
TNQWLGYMPE AIVESTKWWG NTGNAENKPI NFFRLTTRGG LVYDVPIITH EGAIPGGQYL
PFAKGLLADK PSYTVYRNRH YIYRIKTLPD KIEVKYSICD WNIVTNDTYM GYGYNVGVDE
QGNVTITNTM QNCDPHVVRL VAKNGAYFGS QPTDTSVEFT ELANGASQTF KVNKDAVAVG
SAYLEVYYNP DLNATGVVPD KVFIKK
//
