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 18-JAN-2017, entry version 35. 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 / OS JCM 12257 / NCTC 11834 / 2561). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; 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 / RC 2561 {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 RT strain ATCC 33277 and genomic comparison with strain W83 revealed RT extensive genome rearrangements in P. gingivalis."; RL DNA Res. 15:215-225(2008). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND RP SUBUNIT. RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / RC 2561 {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., RA Yoshimura F.; RT "Anchoring and length regulation of Porphyromonas gingivalis Mfa1 RT fimbriae 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 / RC 2561 {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 RT Porphyromonas 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 / RC 2561 {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 RT 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 / RC 2561 {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 RT Porphyromonas gingivalis."; RL PLoS ONE 10:E0139454-E0139454(2015). CC -!- FUNCTION: Tip subunit of the minor fimbriae. These filamentous CC pili are attached to the cell surface; they mediate biofilm CC formation, adhesion onto host cells and onto other bacteria that CC are part of the oral microbiome (PubMed:24118823, CC PubMed:26001707). They play an important role in invasion of CC periodontal tissues and are recognized as major virulence factors. CC Fimbrium subunits from different strains have highly divergent CC 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, CC and the accessory subunits Mfa3, Mfa4 and Mfa5 (PubMed:19589838, CC PubMed:24118823, PubMed:26001707). Fimbrium assembly occurs by CC linear, head-to-tail oligomerization of fimbrial subunits. This is CC mediated via insertion of a C-terminal beta-strand from one CC subunit into a groove in the N-terminal domain of the following CC subunit (Probable). Mfa3 is required for Mfa4 and Mfa5 insertion CC into the fimbrium (PubMed:24118823). {ECO:0000269|PubMed:19589838, CC ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707, CC ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:19589838, CC ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707}. Cell CC outer membrane {ECO:0000269|PubMed:24118823, CC ECO:0000269|PubMed:26437277}. Note=Targeted to the outer membrane CC as a palmitoylated precursor. The lipid modification is no longer CC present after proteolytic processing to the mature form CC (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 CC the abundance of the protein, but is derived from the greater CC length of the major fimbriae. In strain ATCC 33277 and strain ATCC CC BAA-1703 / FDC 381, major fimbriae are 300 - 1600 nM in length and CC about 5 nm in diameter. In contrast, minor fimbriae are only about CC 80 - 120 nm long. This length difference is observed only in a CC small number of strains, including strain ATCC 33277 and strain CC ATCC BAA-1703 / FDC 381, and is due to a loss of function mutation CC in FimB, a protein that restricts fimbrial length in other CC 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; NC_010729.1. DR STRING; 431947.PGN_0289; -. DR EnsemblBacteria; BAG32808; BAG32808; PGN_0289. DR GeneID; 29255535; -. DR KEGG; pgn:PGN_0289; -. DR PATRIC; 22973512; VBIPorGin26334_0287. DR eggNOG; ENOG4106HJD; Bacteria. DR eggNOG; ENOG410Y3YK; LUCA. DR HOGENOM; HOG000059746; -. DR OMA; ITHEGAI; -. DR BioCyc; PGIN431947:GC9J-302-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 GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR014941; FimB/Mfa2/Mfa3. DR Pfam; PF08842; Mfa2; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Direct protein sequencing; KW Fimbrium; Lipoprotein; Membrane; Palmitate; Signal; Virulence. FT SIGNAL 1 20 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT PROPEP 21 43 {ECO:0000269|PubMed:24118823}. FT /FTId=PRO_0000436795. FT CHAIN 44 446 Minor fimbrium tip subunit Mfa3. FT /FTId=PRO_5002781645. FT LIPID 21 21 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 21 21 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. 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 //