MFA2_PORG3
ID MFA2_PORG3 Reviewed; 324 AA.
AC B2RHG2; C6KXN1;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Minor fimbrium anchoring subunit Mfa2 {ECO:0000305};
DE AltName: Full=Minor fimbrial antigen 2;
DE Flags: Precursor;
GN Name=mfa2; OrderedLocusNames=PGN_0288 {ECO:0000312|EMBL:BAG32807.1};
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:BAG32807.1, ECO:0000312|Proteomes:UP000008842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000312|Proteomes:UP000008842};
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP INTERACTION WITH MFA1, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:19589838};
RX PubMed=19589838; DOI=10.1099/mic.0.028928-0;
RA Hasegawa Y., Iwami J., Sato K., Park Y., Nishikawa K., Atsumi T.,
RA Moriguchi K., Murakami Y., Lamont R.J., Nakamura H., Ohno N., Yoshimura F.;
RT "Anchoring and length regulation of Porphyromonas gingivalis Mfa1 fimbriae
RT by the downstream gene product Mfa2.";
RL Microbiology 155:3333-3347(2009).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:26437277};
RX PubMed=26437277; DOI=10.1371/journal.pone.0139454;
RA Ikai R., Hasegawa Y., Izumigawa M., Nagano K., Yoshida Y., Kitai N.,
RA Lamont R.J., Yoshimura F., Murakami Y.;
RT "Mfa4, an accessory protein of Mfa1 fimbriae, modulates fimbrial
RT biogenesis, cell auto-aggregation, and biofilm formation in Porphyromonas
RT gingivalis.";
RL PLoS ONE 10:E0139454-E0139454(2015).
RN [4]
RP SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-29, MUTAGENESIS OF CYS-29, AND
RP LACK OF A CLEAVABLE PROPEPTIDE.
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561
RC {ECO:0000303|PubMed:27062925};
RX PubMed=27062925; DOI=10.1016/j.cell.2016.03.016;
RA Xu Q., Shoji M., Shibata S., Naito M., Sato K., Elsliger M.A., Grant J.C.,
RA Axelrod H.L., Chiu H.J., Farr C.L., Jaroszewski L., Knuth M.W.,
RA Deacon A.M., Godzik A., Lesley S.A., Curtis M.A., Nakayama K., Wilson I.A.;
RT "A distinct type of pilus from the human microbiome.";
RL Cell 165:690-703(2016).
CC -!- FUNCTION: Anchoring subunit of the minor fimbriae. Regulates fimbrial
CC length (PubMed:19589838). 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:19589838, ECO:0000305}.
CC -!- SUBUNIT: Mfa2 is not part of the fimbrium itself, but anchors the
CC fimbrium in the outer membrane via its interaction with Mfa1
CC (PubMed:19589838). Linear, head-to-tail oligomerization of fimbrial
CC subunits mediates assembly of the fimbrium stalk, while the minor
CC components Mfa3, Mfa4 and Mfa5 probably form the fimbrium tip
CC (PubMed:27062925). The anchoring subunit Mfa2 limits fimbrium length
CC and is important for solid fimbrium attachment to the outer membrane.
CC In its absence, the minor fimbriae become very long and are easily
CC detached from the membrane (PubMed:19589838).
CC {ECO:0000269|PubMed:19589838, ECO:0000305|PubMed:27062925}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:19589838,
CC ECO:0000269|PubMed:26437277, ECO:0000269|PubMed:27062925}; Lipid-anchor
CC {ECO:0000305|PubMed:27062925}.
CC -!- PTM: Palmitoylated. Palmitoylation is important for export to the outer
CC membrane. {ECO:0000269|PubMed:27062925}.
CC -!- PTM: Unlike other fimbrial subunits, does not contain a propeptide that
CC is cleaved by gingipain. {ECO:0000269|PubMed:27062925}.
CC -!- DISRUPTION PHENOTYPE: Minor fimbriae are longer than normal and are
CC easily detached from the cell by mild shear stress.
CC {ECO:0000269|PubMed:19589838}.
CC -!- MISCELLANEOUS: The name (minor 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; AP009380; BAG32807.1; -; Genomic_DNA.
DR EMBL; AB360435; BAH90730.1; -; Genomic_DNA.
DR PDB; 5NFI; X-ray; 2.51 A; B=40-320.
DR PDBsum; 5NFI; -.
DR AlphaFoldDB; B2RHG2; -.
DR SMR; B2RHG2; -.
DR STRING; 431947.PGN_0288; -.
DR PRIDE; B2RHG2; -.
DR EnsemblBacteria; BAG32807; BAG32807; PGN_0288.
DR KEGG; pgn:PGN_0288; -.
DR eggNOG; ENOG5033NRG; Bacteria.
DR HOGENOM; CLU_862377_0_0_10; -.
DR OMA; NHDFTIE; -.
DR BioCyc; PGIN431947:G1G2V-315-MON; -.
DR Proteomes; UP000008842; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:UniProtKB.
DR GO; GO:0009297; P:pilus assembly; IMP:UniProtKB.
DR InterPro; IPR014941; FimB/Mfa2/Mfa3.
DR Pfam; PF08842; Mfa2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Signal; Virulence.
FT SIGNAL 1..28
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 29..324
FT /note="Minor fimbrium anchoring subunit Mfa2"
FT /id="PRO_0000436794"
FT LIPID 29
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:27062925"
FT LIPID 29
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 29
FT /note="C->A: Loss of palmitoylation. Abolishes export to
FT the outer membrane."
FT /evidence="ECO:0000269|PubMed:27062925"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:5NFI"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:5NFI"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:5NFI"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:5NFI"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:5NFI"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 288..297
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:5NFI"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:5NFI"
SQ 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
