ID   MFA53_PORGN             Reviewed;         498 AA.
AC   P81363; Q9RM67;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 2.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Minor fimbrium subunit Mfa1 {ECO:0000305};
DE   AltName: Full=53 kDa major outer membrane protein;
DE   Flags: Precursor;
GN   Name=mfa1 {ECO:0000305};
OS   Porphyromonas gingivalis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=837;
RN   [1] {ECO:0000312|EMBL:BAA84008.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-1703 / FDC 381 {ECO:0000312|EMBL:BAA84008.1};
RX   PubMed=9569663;
RA   Hongyo H., Kurihara H., Kokeguchi S., Miyamoto M., Maeda H., Hayakawa M.,
RA   Abiko Y., Takashiba S., Murayama Y.;
RT   "Molecular cloning and characterization of the gene encoding 53 kD outer
RT   membrane protein of Porphyromonas gingivalis.";
RL   Microbios 92:47-57(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 51-75.
RC   STRAIN=A7A-28;
RA   Sojar H.T., Genco R.J.;
RL   Submitted (MAY-1998) to UniProtKB.
RN   [3]
RP   PROTEIN SEQUENCE OF 51-71, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC BAA-1703 / FDC 381;
RX   PubMed=8208139;
RA   Kokeguchi S., Miyamoto M., Ohyama H., Hongyo H., Takigawa M., Kurihara H.,
RA   Murayama Y., Kato K.;
RT   "Biochemical properties of the major outer membrane proteins of
RT   Porphyromonas gingivalis.";
RL   Microbios 77:247-252(1994).
RN   [4]
RP   IDENTIFICATION.
RC   STRAIN=ATCC BAA-1703 / FDC 381;
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. These filamentous
CC       pili are attached to the cell surface; they mediate biofilm formation,
CC       adhesion onto host cells and onto other bacteria that are part of the
CC       oral microbiome. They play an important role in invasion of periodontal
CC       tissues and are recognized as major virulence factors. Mfa1 orthologs
CC       from different strains have highly divergent sequences, and this
CC       correlates with pathogenicity. {ECO:0000250|UniProtKB:B2RHG1}.
CC   -!- SUBUNIT: Structural component of the fimbrial stalk. Minor fimbriae are
CC       composed of a structural subunit, most often Mfa1, and the accessory
CC       subunits Mfa3, Mfa4 and Mfa5. Mfa1 interacts with Mfa2; this anchors
CC       the fimbrium in the membrane. Fimbrium assembly occurs by linear, head-
CC       to-tail oligomerization of fimbrial subunits. This is mediated via
CC       insertion of a C-terminal beta-strand from one subunit into a groove in
CC       the N-terminal domain of the following subunit.
CC       {ECO:0000250|UniProtKB:B2RHG1}.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250|UniProtKB:B2RHG1}. Cell
CC       outer membrane {ECO:0000269|PubMed:8208139}. Note=Probably synthesized
CC       as a palmitoylated precursor. Efficient export to the outer membrane
CC       and integration into fimbriae requires lipidation and subsequent
CC       proteolytic removal of the lipidated propeptide.
CC       {ECO:0000305|PubMed:8208139}.
CC   -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC       FimA/Mfa1 family. {ECO:0000305}.
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DR   EMBL; D31835; BAA84008.1; -; Genomic_DNA.
DR   AlphaFoldDB; P81363; -.
DR   SMR; P81363; -.
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; Direct protein sequencing; Fimbrium; Lipoprotein;
KW   Membrane; Palmitate; Signal; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   PROPEP          20..50
FT                   /evidence="ECO:0000269|PubMed:8208139, ECO:0000269|Ref.2"
FT                   /id="PRO_0000436793"
FT   CHAIN           51..498
FT                   /note="Minor fimbrium subunit Mfa1"
FT                   /id="PRO_0000058042"
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;  53582 MW;  ECEED2CAE848AB1B CRC64;
     MKLNKMFLVG ALLSLGFASC SKEGNGPAPD SSSTADTHMS VSMSLPQHNR AGDNDYNPIG
     EYGGVDKIND LTVYVVGDGK IDVRKLSTAD LQVNQGASTT SIVTAPFQVK SGEKTVYAIV
     NITPKVEAAL NAATNAADLK VAYEAAYAAF SDAGSEIATL VNNQDQMIMS GKPVVQTILA
     NVSAANASVQ NKVPIIVKRA AIRASMTITQ QPVNGAYEIK ALRPGNVEVG IATVSDLKWA
     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