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 29-SEP-2021, entry version 46. 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; Bacteroidetes; 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}. 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; 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 SMR; B2RHG3; -. DR STRING; 431947.PGN_0289; -. DR EnsemblBacteria; BAG32808; BAG32808; PGN_0289. DR GeneID; 29255535; -. DR KEGG; pgn:PGN_0289; -. DR eggNOG; ENOG502ZBHU; Bacteria. DR HOGENOM; CLU_051995_0_0_10; -. DR OMA; GEESINM; -. 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 //