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Minor fimbrium anchoring subunit Mfa2 (Minor fimbrial antigen 2)

 MFA2_PORG3              Reviewed;         324 AA.
B2RHG2; C6KXN1;
06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 1.
07-JUN-2017, entry version 34.
RecName: Full=Minor fimbrium anchoring subunit Mfa2 {ECO:0000305};
AltName: Full=Minor fimbrial antigen 2;
Flags: Precursor;
Name=mfa2; OrderedLocusNames=PGN_0288 {ECO:0000312|EMBL:BAG32807.1};
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 /
JCM 12257 / NCTC 11834 / 2561).
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
Porphyromonadaceae; Porphyromonas.
NCBI_TaxID=431947;
[1] {ECO:0000312|EMBL:BAG32807.1, ECO:0000312|Proteomes:UP000008842}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561 {ECO:0000312|Proteomes:UP000008842};
PubMed=18524787; DOI=10.1093/dnares/dsn013;
Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
Nakayama K.;
"Determination of the genome sequence of Porphyromonas gingivalis
strain ATCC 33277 and genomic comparison with strain W83 revealed
extensive genome rearrangements in P. gingivalis.";
DNA Res. 15:215-225(2008).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, INTERACTION WITH MFA1, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561 {ECO:0000303|PubMed:19589838};
PubMed=19589838; DOI=10.1099/mic.0.028928-0;
Hasegawa Y., Iwami J., Sato K., Park Y., Nishikawa K., Atsumi T.,
Moriguchi K., Murakami Y., Lamont R.J., Nakamura H., Ohno N.,
Yoshimura F.;
"Anchoring and length regulation of Porphyromonas gingivalis Mfa1
fimbriae by the downstream gene product Mfa2.";
Microbiology 155:3333-3347(2009).
[3]
SUBCELLULAR LOCATION.
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561 {ECO:0000303|PubMed:26437277};
PubMed=26437277; DOI=10.1371/journal.pone.0139454;
Ikai R., Hasegawa Y., Izumigawa M., Nagano K., Yoshida Y., Kitai N.,
Lamont R.J., Yoshimura F., Murakami Y.;
"Mfa4, an accessory protein of Mfa1 fimbriae, modulates fimbrial
biogenesis, cell auto-aggregation, and biofilm formation in
Porphyromonas gingivalis.";
PLoS ONE 10:E0139454-E0139454(2015).
[4]
SUBCELLULAR LOCATION, PALMITOYLATION, MUTAGENESIS OF CYS-29, AND LACK
OF A CLEAVABLE PROPAPTIDE.
STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
2561 {ECO:0000303|PubMed:27062925};
PubMed=27062925; DOI=10.1016/j.cell.2016.03.016;
Xu Q., Shoji M., Shibata S., Naito M., Sato K., Elsliger M.A.,
Grant J.C., Axelrod H.L., Chiu H.J., Farr C.L., Jaroszewski L.,
Knuth M.W., Deacon A.M., Godzik A., Lesley S.A., Curtis M.A.,
Nakayama K., Wilson I.A.;
"A distinct type of pilus from the human microbiome.";
Cell 165:690-703(2016).
-!- FUNCTION: Anchoring subunit of the minor fimbriae. Regulates
fimbrial length (PubMed:19589838). These 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. Fimbriae of P.gingivalis are major virulence
factors (Probable). {ECO:0000269|PubMed:19589838, ECO:0000305}.
-!- SUBUNIT: Mfa2 is not part of the fimbrium itself, but anchors the
fimbrium in the outer membrane via its interaction with Mfa1
(PubMed:19589838). Linear, head-to-tail oligomerization of
fimbrial subunits mediates assembly of the fimbrium stalk, while
the minor components Mfa3, Mfa4 and Mfa5 probably form the
fimbrium tip (PubMed:27062925). The anchoring subunit Mfa2 limits
fimbrium length and is important for solid fimbrium attachment to
the outer membrane. In its absence, the minor fimbriae become very
long and are easily detached from the membrane (PubMed:19589838).
{ECO:0000269|PubMed:19589838, ECO:0000305|PubMed:27062925}.
-!- SUBCELLULAR LOCATION: Cell outer membrane
{ECO:0000269|PubMed:19589838, ECO:0000269|PubMed:26437277,
ECO:0000269|PubMed:27062925}; Lipid-anchor
{ECO:0000305|PubMed:27062925}.
-!- PTM: Palmitoylated. Palmitoylation is important for export to the
outer membrane. {ECO:0000269|PubMed:27062925}.
-!- PTM: Unlike other fimbrial subunits, does not contain a propeptide
that is cleaved by gingipain. {ECO:0000269|PubMed:27062925}.
-!- DISRUPTION PHENOTYPE: Minor fimbriae are longer than normal and
are easily detached from the cell by mild shear stress.
{ECO:0000269|PubMed:19589838}.
-!- MISCELLANEOUS: The name (minor 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 ATCC
BAA-1703 / FDC 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
ATCC BAA-1703 / FDC 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.
FimB/Mfa2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AP009380; BAG32807.1; -; Genomic_DNA.
EMBL; AB360435; BAH90730.1; -; Genomic_DNA.
SMR; B2RHG2; -.
STRING; 431947.PGN_0288; -.
EnsemblBacteria; BAG32807; BAG32807; PGN_0288.
KEGG; pgn:PGN_0288; -.
eggNOG; ENOG4106RSZ; Bacteria.
eggNOG; ENOG410YJ58; LUCA.
OMA; QGSYQFV; -.
BioCyc; PGIN431947:GC9J-301-MONOMER; -.
Proteomes; UP000008842; Chromosome.
GO; GO:0009279; C:cell outer membrane; IDA:UniProtKB.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0009297; P:pilus assembly; IMP:UniProtKB.
InterPro; IPR014941; FimB/Mfa2/Mfa3.
Pfam; PF08842; Mfa2; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
Cell outer membrane; Complete proteome; Lipoprotein; Membrane;
Palmitate; Signal; Virulence.
SIGNAL 1 28 {ECO:0000255|PROSITE-ProRule:PRU00303}.
CHAIN 29 324 Minor fimbrium anchoring subunit Mfa2.
/FTId=PRO_0000436794.
LIPID 29 29 N-palmitoyl cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303,
ECO:0000269|PubMed:27062925}.
LIPID 29 29 S-diacylglycerol cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
MUTAGEN 29 29 C->A: Loss of palmitoylation. Abolishes
export to the outer membrane.
{ECO:0000269|PubMed:27062925}.
SEQUENCE 324 AA; 36862 MW; B930626ED6D340D9 CRC64;
MNKRKHMDIR RLIISLPAIM ALWGGLASCD KMIYDNYDDC PRGVYVNFYS QTECAENPSY
PAEVARLNVY AFDKDGILRS ANVFEDVQLS AAKEWLIPLE KDGLYTIFAW GNIDDHYNIG
EIKIGETTKQ QVLMRLKQDG KWATNIDGTT LWYATSPVVE LKNMEDGADQ YIHTRANLRE
YTNRVTVSVD SLPHPENYEI KLASSNGSYR FDGTVAKADS TYYPGETKVV GDSTCRAFFT
TLKLESGHEN TLSVTHKPTG REIFRTDLVG AILSSQYAQN INLRCINDFD IRLVAHHCNC
PDDTYVVVQI WINGWLIHSY EIEL


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