MFA4_PORG3
ID MFA4_PORG3 Reviewed; 333 AA.
AC B2RHG4;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Minor fimbrium tip subunit MfA4 {ECO:0000303|PubMed:26972441};
DE AltName: Full=Immunoreactive 32 kDa antigen {ECO:0000312|EMBL:BAG32809.1};
DE Flags: Precursor;
GN OrderedLocusNames=PGN_0290 {ECO:0000312|EMBL:BAG32809.1};
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:BAG32809.1, 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 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 [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 PROTEIN SEQUENCE OF 54-63, PROPEPTIDE, SUBCELLULAR LOCATION, SUBUNIT, AND
RP DISRUPTION PHENOTYPE.
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 26-333, PROTEIN SEQUENCE OF
RP N-TERMINUS, PROPEPTIDE, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF
RP ARG-53.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:26972441};
RX PubMed=26972441; DOI=10.1038/srep22945;
RA Kloppsteck P., Hall M., Hasegawa Y., Persson K.;
RT "Structure of the fimbrial protein Mfa4 from Porphyromonas gingivalis in
RT its precursor form: implications for a donor-strand complementation
RT mechanism.";
RL Sci. Rep. 6:22945-22945(2016).
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:19589838, PubMed:26001707). They play an important
CC role in invasion of periodontal tissues and are recognized as major
CC virulence factors (Probable). {ECO:0000269|PubMed:19589838,
CC ECO:0000269|PubMed:26001707, ECO:0000305}.
CC -!- SUBUNIT: Component of the fimbrium tip. Minor fimbriae are composed of
CC a structural subunit, most often Mfa1, and the accessory subunits Mfa3,
CC Mfa4 and Mfa5 (PubMed:19589838, PubMed:24118823, PubMed:26001707,
CC PubMed:26437277, PubMed:26972441). Mfa4 is required for Mfa3 and Mfa5
CC insertion into the fimbrium (PubMed:26437277). Fimbrium assembly occurs
CC by linear, head-to-tail oligomerization of fimbrial subunits. This is
CC mediated via insertion of a C-terminal beta-strand from one subunit
CC into a groove in the N-terminal domain of the following subunit
CC (PubMed:26972441). {ECO:0000269|PubMed:19589838,
CC ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707,
CC ECO:0000269|PubMed:26437277, ECO:0000269|PubMed:26972441, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:19589838,
CC ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707,
CC ECO:0000269|PubMed:26437277, ECO:0000269|PubMed:26972441}. Cell outer
CC membrane {ECO:0000269|PubMed:26437277}. Note=Targeted to the outer
CC membrane as a palmitoylated precursor. The lipid modification is no
CC longer present after proteolytic processing to the mature form.
CC {ECO:0000305|PubMed:26437277, ECO:0000305|PubMed:26972441}.
CC -!- DISRUPTION PHENOTYPE: No effect on autoaggregation.
CC {ECO:0000269|PubMed:26437277}.
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 FimA/Mfa1 family. {ECO:0000305}.
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DR EMBL; AP009380; BAG32809.1; -; Genomic_DNA.
DR RefSeq; WP_012457398.1; NZ_CP025930.1.
DR PDB; 5DHM; X-ray; 1.90 A; A/B=26-333.
DR PDBsum; 5DHM; -.
DR AlphaFoldDB; B2RHG4; -.
DR SMR; B2RHG4; -.
DR STRING; 431947.PGN_0290; -.
DR PRIDE; B2RHG4; -.
DR EnsemblBacteria; BAG32809; BAG32809; PGN_0290.
DR GeneID; 29255536; -.
DR KEGG; pgn:PGN_0290; -.
DR eggNOG; ENOG502ZAWJ; Bacteria.
DR HOGENOM; CLU_833813_0_0_10; -.
DR OMA; GANPAKY; -.
DR BioCyc; PGIN431947:G1G2V-317-MON; -.
DR Proteomes; UP000008842; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IDA:UniProtKB.
DR InterPro; IPR029141; FimA_N.
DR Pfam; PF06321; P_gingi_FimA; 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..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 19..53
FT /evidence="ECO:0000269|PubMed:26437277,
FT ECO:0000269|PubMed:26972441"
FT /id="PRO_0000436796"
FT CHAIN 54..333
FT /note="Minor fimbrium tip subunit MfA4"
FT /id="PRO_0000436797"
FT SITE 53..54
FT /note="Cleavage; by gingipain"
FT /evidence="ECO:0000269|PubMed:26972441"
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 53
FT /note="R->A: Abolishes cleavage site."
FT /evidence="ECO:0000269|PubMed:26972441"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:5DHM"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:5DHM"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:5DHM"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:5DHM"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:5DHM"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:5DHM"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5DHM"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:5DHM"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 170..189
FT /evidence="ECO:0007829|PDB:5DHM"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 204..216
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:5DHM"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:5DHM"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 272..282
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:5DHM"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:5DHM"
SQ SEQUENCE 333 AA; 37110 MW; 9600624B8E1E6A26 CRC64;
MKKYLLYASL LTSVLLFSCS KNNPSEPVED RSIEISIRVD DFTKTGETVR YERNQGSAAE
RLITNLYLLL FDQSGANPAK YYIAGNTFSG GIWLPDDMKV KLDMTQSEAG ERKVYVVANV
DNAVKTALDA VANESDLQTV KRTTAMPWST DIASPFLMSG NKTHDFLANR LLDNVPLVRA
IAKVELNISL SEKFQIVPII VNGSLSEFKF RYVNFDKETY VVKPTTKPDN LISSANGVWP
QITDWTVWGA SLNTSPAPDA GTGYTLDANG KVTALRIVTY LNERDSKGAT VEVALPRVDD
GTLPPPEFGP ELYRLPLPDK ILRNHWYKYE VEI
