ID   MFA1_PORGN              Reviewed;         498 AA.
AC   P0DOA1;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Minor fimbrium subunit Mfa1 {ECO:0000305};
DE   AltName: Full=53 kDa fimbrilin;
DE   Flags: Precursor;
GN   Name=mfa1 {ECO:0000305}; Synonyms=53K {ECO:0000312|EMBL:BAR91678.1};
OS   Porphyromonas gingivalis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=837;
RN   [1] {ECO:0000312|EMBL:BAR91678.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ando {ECO:0000312|EMBL:BAR91678.1};
RA   Nagano K., Hasegawa Y., Yoshida Y., Yoshimura F.;
RT   "Another fimbrilin of Mfa1 fimbriae in Porphyromonas gingivalis.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=Ando {ECO:0000303|PubMed:26001707};
RX   PubMed=26001707; DOI=10.1177/0022034515588275;
RA   Nagano K., Hasegawa Y., Yoshida Y., Yoshimura F.;
RT   "A major fimbrilin variant of Mfa1 fimbriae in Porphyromonas gingivalis.";
RL   J. Dent. Res. 94:1143-1148(2015).
CC   -!- FUNCTION: Structural subunit of the minor fimbriae (PubMed:26001707).
CC       These filamentous pili are attached to the cell surface; they mediate
CC       biofilm formation, adhesion onto host cells and onto other bacteria
CC       that are part of the oral microbiome. They play an important role in
CC       invasion of periodontal tissues and are recognized as major virulence
CC       factors. Mfa1 orthologs from different strains have highly divergent
CC       sequences, and this correlates with pathogenicity (Probable).
CC       {ECO:0000269|PubMed:26001707, ECO:0000305}.
CC   -!- SUBUNIT: Structural component of the fimbrial stalk. Minor fimbriae are
CC       composed of a structural subunit, such as the 53 kDa fimbrillin, and
CC       the accessory subunits Mfa3, Mfa4 and Mfa5 (PubMed:26001707). Fimbrium
CC       assembly occurs by linear, head-to-tail oligomerization of fimbrial
CC       subunits. This is mediated via insertion of a C-terminal beta-strand
CC       from one subunit into a groove in the N-terminal domain of the
CC       following subunit (Probable). {ECO:0000269|PubMed:26001707,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:26001707}. Cell
CC       outer membrane {ECO:0000305}. Note=Probably synthesized as a
CC       palmitoylated precursor. Efficient export to the outer membrane and
CC       integration into fimbriae requires lipidation and subsequent
CC       proteolytic removal of the lipidated propeptide (Probable).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC       FimA/Mfa1 family. {ECO:0000305}.
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DR   EMBL; AB999995; BAR91678.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0DOA1; -.
DR   SMR; P0DOA1; -.
DR   PRIDE; P0DOA1; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019867; C:outer membrane; ISS:UniProtKB.
DR   GO; GO:0009418; C:pilus shaft; ISS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR   InterPro; IPR029140; FimA_C.
DR   Pfam; PF15495; Fimbrillin_C; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Fimbrium; Lipoprotein; Membrane; Palmitate; Signal;
KW   Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   PROPEP          20..50
FT                   /evidence="ECO:0000250|UniProtKB:B2RHG1"
FT                   /id="PRO_0000436792"
FT   CHAIN           51..498
FT                   /note="Minor fimbrium subunit Mfa1"
FT                   /id="PRO_5005907438"
FT   REGION          436..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            50..51
FT                   /note="Cleavage; by gingipain"
FT                   /evidence="ECO:0000250|UniProtKB:B2RHG1"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   498 AA;  53666 MW;  FCE570ADD8430A15 CRC64;
     MKLNKMFLVG ALLSLGFASC SKEGNGPAPD SSSTADTHMS VSMSLPQHNR AGDNDYNPIG
     EYGGVDKIND LTVYVVGDGK IDVRKLSTAD LQVNQGASTT SIVTAPFQVK SGEKTVYAIV
     NITPKVEAAL NAATNAADLK VAYEAAYAAF SDAGSEIATL VNNQDQMIMS GKPVVQTILP
     NVSAANASVQ NKVPIIVKRA AIRASMTITQ QPVNGAYEIK ALRPGNVEVV IATVSDLKWS
     VAQYEKKYYL QQKDNALSPA ASFVPASTND YNGANGAMKH YDYSQLANRI TVHQLNAPYS
     VTDVPNVAYK YVSETTHADN DYRKGNTTYI LVKGKLKPVA AMWADGEQAA YQEGGDLFLG
     LVTGKFYANE ANANAANPAS GGAGNPRVVT YKAAAVYYYA WLNPNTLDPT TWTMSPARRN
     NIYNVNISKF RNIGLSGNPF VPTDPDPNNP DTPDNPDTPD PEDPDTPNPE EPLPVQKTYM
     VVDVTVTPWT LHNYDIEF