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Major fimbrium subunit FimA type-2 (Fimbrillin) (Fimbrilin) (Major fimbrial subunit protein type II)

 FIMA2_PORGN             Reviewed;         384 AA.
Q51822; Q51823; Q51824;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
06-JUL-2016, sequence version 2.
15-MAR-2017, entry version 65.
RecName: Full=Major fimbrium subunit FimA type-2;
AltName: Full=Fimbrillin;
Short=Fimbrilin;
AltName: Full=Major fimbrial subunit protein type II;
Flags: Precursor;
Name=fimA;
Porphyromonas gingivalis.
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
Porphyromonadaceae; Porphyromonas.
NCBI_TaxID=837;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=HW24D1, OMZ314, and OMZ409;
PubMed=7902712; DOI=10.1006/bbrc.1993.2467;
Fujiwara T., Morishima S., Takahashi I., Hamada S.;
"Molecular cloning and sequencing of the fimbrilin gene of
Porphyromonas gingivalis strains and characterization of recombinant
proteins.";
Biochem. Biophys. Res. Commun. 197:241-247(1993).
[2]
PROTEIN SEQUENCE OF 47-58.
PubMed=1987052;
Lee J.Y., Sojar H.T., Bedi G.S., Genco R.J.;
"Porphyromonas (Bacteroides) gingivalis fimbrillin: size, amino-
terminal sequence, and antigenic heterogeneity.";
Infect. Immun. 59:383-389(1991).
[3]
FUNCTION, AND CLASSIFICATION INTO TYPES.
PubMed=11748193; DOI=10.1128/IAI.70.1.277-285.2002;
Nakagawa I., Amano A., Kuboniwa M., Nakamura T., Kawabata S.,
Hamada S.;
"Functional differences among FimA variants of Porphyromonas
gingivalis and their effects on adhesion to and invasion of human
epithelial cells.";
Infect. Immun. 70:277-285(2002).
[4]
CLASSIFICATION.
PubMed=23809984; DOI=10.1111/omi.12032;
Nagano K., Abiko Y., Yoshida Y., Yoshimura F.;
"Genetic and antigenic analyses of Porphyromonas gingivalis FimA
fimbriae.";
Mol. Oral. Microbiol. 28:392-403(2013).
-!- FUNCTION: Structural subunit of the major fimbriae (Probable).
These long, filamentous pili are attached to the cell surface;
they mediate biofilm formation, adhesion onto host cells and onto
other bacteria that are part of the oral microbiome. They play an
important role in the invasion of periodontal tissues. Fimbriae
and their constituents are major virulence factors. FimA proteins
from different strains have highly divergent sequences, and this
has been used for classification. The sequence-based
classification correlates with pathogenicity.
{ECO:0000269|PubMed:11748193, ECO:0000305}.
-!- SUBUNIT: Fimbriae are composed of a major, structural subunit
(FimA) and the minor components FimC, FimD and FimE (By
similarity). Head-to-tail oligomerization of FimA molecules
mediates assembly of the fimbrium stalk, while the minor
components probably form the fimbrium tip. Linear, head-to-tail
oligomerization of FimA is mediated by a conformation change,
facilitating the insertion of a C-terminal beta-strand into a
groove in the N-terminal domain of the following subunit (By
similarity). {ECO:0000250|UniProtKB:B2RH54,
ECO:0000250|UniProtKB:P59914}.
-!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250|UniProtKB:B2RH54}.
Cell outer membrane {ECO:0000250|UniProtKB:B2RH54}.
Note=Synthesized as palmitoylated precursor. The lipidated
propeptide is removed during processing to the mature protein.
{ECO:0000250|UniProtKB:B2RH54}.
-!- PTM: Synthesized as palmitoylated lipoprotein precursor. Efficient
export to the outer membrane and integration into fimbriae
requires lipidation and subsequent proteolytic removal of the
lipidated propeptide. {ECO:0000250|UniProtKB:B2RH54}.
-!- MISCELLANEOUS: The name (major fimbrium subunit) does not indicate
the abundance of the protein, but is derived from the greater
length of the major fimbriae. In strain ATCC 33277 and strain 381,
major fimbriae are 300 - 1600 nM in length and about 5 nm in
diameter. In contrast, minor fimbriae are only about 80 - 120 nm
long. This length difference is observed only in a small number of
strains, including strain ATCC 33277 and strain 381, and is due to
a loss of function mutation in FimB, a protein that restricts
fimbrial length in other strains. {ECO:0000305}.
-!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
FimA/Mfa1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA04623.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA04624.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA04625.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; D17797; BAA04623.1; ALT_INIT; Genomic_DNA.
EMBL; D17798; BAA04624.1; ALT_INIT; Genomic_DNA.
EMBL; D17799; BAA04625.1; ALT_INIT; Genomic_DNA.
PIR; JN0916; JN0916.
PIR; JN0918; JN0918.
SMR; Q51822; -.
PRIDE; Q51822; -.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0009289; C:pilus; ISS:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
InterPro; IPR029141; FimA_N.
InterPro; IPR008110; Fimbrillin.
Pfam; PF06321; P_gingi_FimA; 1.
PRINTS; PR01737; FIMBRILLIN.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
Cell adhesion; Cell outer membrane; Direct protein sequencing;
Fimbrium; Lipoprotein; Membrane; Palmitate; Signal; Virulence.
SIGNAL 1 18 {ECO:0000255|PROSITE-ProRule:PRU00303}.
PROPEP 19 46 {ECO:0000269|PubMed:1987052}.
/FTId=PRO_0000009160.
CHAIN 47 384 Major fimbrium subunit FimA type-2.
/FTId=PRO_0000009161.
REGION 375 384 Important for oligomerization and
fimbrium assembly.
{ECO:0000250|UniProtKB:P59914}.
SITE 46 47 Cleavage; by gingipain.
{ECO:0000250|UniProtKB:B2RH54}.
LIPID 19 19 N-palmitoyl cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
LIPID 19 19 S-diacylglycerol cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
VARIANT 100 104 EMKLA -> AMELV (in strain: OMZ409).
VARIANT 126 126 A -> T (in strain: OMZ409).
VARIANT 136 136 E -> D (in strain: OMZ409).
SEQUENCE 384 AA; 41869 MW; 3CB4EFC46E842F5A CRC64;
MKKTKFFLLG LAALAMTACN KDNEAEPVTE GNATISVVLK TSNPNRAFGE DESKVAKLTV
MVYNGEQQEA IKSAENATKV EDIKCSAGQR TLVVMANTGE MKLAGKTLAE VKALTTELTA
ENQEAAGLIM TAEPVEVTLV AGNNYYGYDG SQGGNQISQD TPLEIKRVHA RMAFTEIKVQ
MSPSYVNKYN FAPENIYALV AKKESNLFGA SLANSDDAYL TGSLTNFNGA YSPANYTHVD
WLGRDYTEPS NNAPQGFYVL ESTYAQNAGL RPTILCVKGK LTKHDGTPLS SEEMTAAFNA
GWIVADNNPT TYYPVLVNFN SNNYTYDNGY TPKNKIERNH KYDIKLTITG PGTNNPENPI
TESAHLNVQC TVAEWVLVGQ NATW


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