ID   FIMB_PORGI              Reviewed;         303 AA.
AC   Q7MT55;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Major fimbrium anchoring subunit FimB;
DE   Flags: Precursor;
GN   Name=fimB {ECO:0000305};
GN   OrderedLocusNames=PG_2133 {ECO:0000312|EMBL:AAQ67088.1};
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619 {ECO:0000312|EMBL:AAQ67088.1};
RN   [1] {ECO:0000312|EMBL:AAQ67088.1, ECO:0000312|Proteomes:UP000000588}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83 {ECO:0000312|Proteomes:UP000000588};
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
RN   [2]
RP   IDENTIFICATION, SUBCELLULAR LOCATION, AND FUNCTION.
RC   STRAIN=OMZ314 {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. These filamentous pili are attached to the cell surface; they
CC       mediate biofilm formation, adhesion onto host cells and onto other
CC       bacteria that are part of the oral microbiome. Fimbriae of P.gingivalis
CC       are major virulence factors. {ECO:0000250|UniProtKB:A0PA81}.
CC   -!- SUBUNIT: FimB is not part of the fimbrium itself, but anchors the
CC       fimbrium in the outer membrane. Linear, head-to-tail oligomerization of
CC       fimbrial subunits mediates assembly of the fimbrium stalk, while the
CC       minor components FimC, FimD and FimE probably form the fimbrium tip.
CC       The anchoring subunit FimB limits fimbrium length and is important for
CC       solid fimbrium attachment to the outer membrane. In its absence, the
CC       major fimbriae become very long and are easily detached from the
CC       membrane. {ECO:0000250|UniProtKB:A0PA81}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000250|UniProtKB:A0PA81}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:A0PA81, 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}.
CC   -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC       FimB/Mfa2 family. {ECO:0000305}.
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DR   EMBL; AE015924; AAQ67088.1; -; Genomic_DNA.
DR   RefSeq; WP_005873477.1; NC_002950.2.
DR   AlphaFoldDB; Q7MT55; -.
DR   SMR; Q7MT55; -.
DR   STRING; 242619.PG_2133; -.
DR   EnsemblBacteria; AAQ67088; AAQ67088; PG_2133.
DR   KEGG; pgi:PG_2133; -.
DR   PATRIC; fig|242619.8.peg.1987; -.
DR   eggNOG; ENOG503429A; Bacteria.
DR   HOGENOM; CLU_078506_0_0_10; -.
DR   OMA; ASMNITI; -.
DR   OrthoDB; 1893723at2; -.
DR   BioCyc; PGIN242619:G1G02-2003-MON; -.
DR   Proteomes; UP000000588; Chromosome.
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; Reference proteome;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..303
FT                   /note="Major fimbrium anchoring subunit FimB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_0000436789"
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;  33839 MW;  561FBA26FB7B5F04 CRC64;
     MNDAKKYIVS VLILLVAGMF GGCIKEDYSD CPRPFRLTVR AWDADMQDIT ETGAVQRVVI
     FVFDETGRRI DRLMMDAAQV AARKPIPLEY DGPTTVSFVA WANPDDHMLE ETANVQNVKD
     LFFRLSSTDG IAQSPGDLFS GVLTCPIEYG SIEQGTDQTV DIYRRTAQVH IIIRGYQEWL
     EANGPRQLPD YADILLGETP DTYTGLAELI GNAVQYRPDG QIQNGDFISP IFRVYPTLDT
     TPLHLKLYAY GQELLNISTG SDGVPFIPVI GKMLNIYIDL RGANLNVLVS VTPWDVVQQY
     AEY