ID   FIMB_PORG3              Reviewed;         303 AA.
AC   A0PA81;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Major fimbrium anchoring subunit FimB {ECO:0000305};
DE   Flags: Precursor;
GN   Name=fimB {ECO:0000305};
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:BAF37090.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC   {ECO:0000312|EMBL:BAF37090.1};
RX   PubMed=17081195; DOI=10.1111/j.1462-5822.2006.00825.x;
RA   Kato T., Kawai S., Nakano K., Inaba H., Kuboniwa M., Nakagawa I., Tsuda K.,
RA   Omori H., Ooshima T., Yoshimori T., Amano A.;
RT   "Virulence of Porphyromonas gingivalis is altered by substitution of
RT   fimbria gene with different genotype.";
RL   Cell. Microbiol. 9:753-765(2007).
RN   [2]
RP   SUBCELLULAR LOCATION, FUNCTION, AND MISCELLANEOUS.
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC   {ECO:0000303|PubMed:20530728};
RX   PubMed=20530728; DOI=10.1177/0022034510370089;
RA   Nagano K., Hasegawa Y., Murakami Y., Nishiyama S., Yoshimura F.;
RT   "FimB regulates FimA fimbriation in Porphyromonas gingivalis.";
RL   J. Dent. Res. 89:903-908(2010).
CC   -!- FUNCTION: Anchoring subunit of the major fimbriae. Regulates fimbrial
CC       length (PubMed:20530728). These filamentous pili are attached to the
CC       cell surface; they mediate biofilm formation, adhesion onto host cells
CC       and onto other bacteria that are part of the oral microbiome. Fimbriae
CC       of P.gingivalis are major virulence factors (Probable).
CC       {ECO:0000269|PubMed:20530728, ECO:0000305}.
CC   -!- SUBUNIT: FimB is not part of the fimbrium itself, but anchors the
CC       fimbrium in the outer membrane (PubMed:20530728). Linear, head-to-tail
CC       oligomerization of fimbrial subunits mediates assembly of the fimbrium
CC       stalk, while the minor components FimC, FimD and FimE probably form the
CC       fimbrium tip (Probable). The anchoring subunit FimB limits fimbrium
CC       length and is important for solid fimbrium attachment to the outer
CC       membrane. In its absence, the major fimbriae become very long and are
CC       easily detached from the membrane (PubMed:20530728). {ECO:0000305,
CC       ECO:0000305|PubMed:20530728}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000305|PubMed:20530728}; Lipid-anchor {ECO:0000305}.
CC   -!- MISCELLANEOUS: The name (major 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|PubMed:20530728}.
CC   -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC       FimB/Mfa2 family. {ECO:0000305}.
CC   -!- CAUTION: According to PubMed:20530728, the fimB gene contains a
CC       premature stop codon that prevents expression of this protein in strain
CC       ATCC 33277 and strain ATCC BAA-1703 / FDC 381. This is the cause for
CC       the production of abnormally long fimbriae by these strains; in vitro
CC       mutagenesis that restores the full open reading frame leads to the
CC       production of shorter fimbriae in strain ATCC 33277 (PubMed:20530728).
CC       In contrast, there is no premature stop codon in the sequence reported
CC       by PubMed:17081195. {ECO:0000305|PubMed:17081195,
CC       ECO:0000305|PubMed:20530728}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=A loosening of habits
CC       - Issue 182 of August 2016;
CC       URL="https://web.expasy.org/spotlight/back_issues/182/";
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DR   EMBL; AB261608; BAF37090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0PA81; -.
DR   SMR; A0PA81; -.
DR   STRING; 431947.PGN_0181; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR014941; FimB/Mfa2/Mfa3.
DR   Pfam; PF08842; Mfa2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Lipoprotein; Membrane; Palmitate; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..303
FT                   /note="Major fimbrium anchoring subunit FimB"
FT                   /id="PRO_0000436787"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   303 AA;  33805 MW;  99ECB6D9087B5F0D CRC64;
     MNDAKKYIVS VLILLVAGMF GGCIKEDYSD CPRPFRLTVR AWDADMQDIT ETGAVQRVVI
     FVFDETGRRI DRLMMDAAQV AARKPIPLEY DGPTTVSFVA WANPDDHMLE ETANVQNVKD
     LFFRLSSTDG IAQSPGDLFS GVLTCPIEYG SIEQGTDQTV DIYRRTAQVH IIIRGYQEWL
     EANGPRQLPD YADILLGETP DTYTGLAELI GNAVQYRPDG QIQNGDFISP IIRVYPTLDT
     TPLHLKLYAY GQELLNISTG SDGVPFIPVI GKMLNIYIDL RGANLNVLVS VTPWDVVQQY
     AEY