ID FIMB_PORGN Reviewed; 305 AA.
AC A0PA72;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE RecName: Full=Major fimbrium anchoring subunit FimB;
DE Flags: Precursor;
GN Name=fimB {ECO:0000305};
OS Porphyromonas gingivalis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=837 {ECO:0000312|EMBL:BAF37081.1};
RN [1] {ECO:0000312|EMBL:BAF37081.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=OMZ314 {ECO:0000312|EMBL:BAF37081.1};
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 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 (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. {ECO:0000305,
CC ECO:0000305|PubMed:20530728}.
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:0000305|PubMed:20530728}; Lipid-anchor
CC {ECO:0000250|UniProtKB:A0PA81}.
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}.
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DR EMBL; AB261607; BAF37081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0PA72; -.
DR SMR; A0PA72; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.2100; -; 1.
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..305
FT /note="Major fimbrium anchoring subunit FimB"
FT /id="PRO_0000436788"
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 305 AA; 34082 MW; 05CDF13FE19B7A7B CRC64;
MNDAKKYIVS VLILLVAGMF GGCIKEDYSD CPRPFRLTVR AWDADMQDIT ETGAVQRVVI
FVFDETGRRI DRLMMDAAQV AARKPIPLEY DGPTTVSFVA WANPDDHMLE ETANVQNVKD
LFFRLSSTDG IAQSPGDLFS GVLTCPIEYG SIEQGTDQTV DIYRRTAQVH IIIRGYQEWL
DANGPRQLPD YADILLGETP DTYTGLAELI GNAVQYRPDG QIQNGDFISP IFRVYPTLDT
TPLHLKLYAY GQELLNISTG SDGVPFIPVI GKMLNIYIDL RGANLNVLVS VTPWDVVQQQ
QYAEY
//
