MFA4_PORGI
ID MFA4_PORGI Reviewed; 333 AA.
AC Q7MXK0;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Minor fimbrium tip subunit MfA4 {ECO:0000303|PubMed:27062925};
DE AltName: Full=Immunoreactive 32 kDa antigen PG49 {ECO:0000303|PubMed:27062925};
DE Flags: Precursor;
GN Name=mfA4; OrderedLocusNames=PG_0181 {ECO:0000312|EMBL:AAQ65416.1};
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619 {ECO:0000312|Proteomes:UP000000588};
RN [1] {ECO:0000312|EMBL:AAQ65416.1, ECO:0000312|Proteomes:UP000000588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000312|Proteomes:UP000000588};
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
RN [2] {ECO:0007744|PDB:4RDB}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 30-333, PROPOSED FUNCTION, AND
RP SUBUNIT.
RC STRAIN=ATCC BAA-308 / W83 {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: Tip subunit of the minor fimbriae (PubMed:27062925). These
CC filamentous pili are attached to the cell surface; they mediate biofilm
CC formation, adhesion onto host cells and onto other bacteria that are
CC part of the oral microbiome. They play an important role in invasion of
CC periodontal tissues and are recognized as major virulence factors
CC (Probable). {ECO:0000250|UniProtKB:B2RHG4,
CC ECO:0000305|PubMed:27062925}.
CC -!- SUBUNIT: Component of the fimbrium tip. Minor fimbriae are composed of
CC a structural subunit, most often Mfa1, and the accessory subunits Mfa3,
CC Mfa4 and Mfa5. Mfa4 is required for Mfa3 and Mfa5 insertion into the
CC fimbrium. Fimbrium assembly occurs by linear, head-to-tail
CC oligomerization of fimbrial subunits. This is mediated via insertion of
CC a C-terminal beta-strand from one subunit into a groove in the N-
CC terminal domain of the following subunit.
CC {ECO:0000250|UniProtKB:B2RHG4, ECO:0000305|PubMed:27062925}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250|UniProtKB:B2RHG4}. Cell
CC outer membrane {ECO:0000250|UniProtKB:B2RHG4}. Note=Targeted to the
CC outer membrane as a palmitoylated precursor. The lipid modification is
CC no longer present after proteolytic processing to the mature form.
CC {ECO:0000250|UniProtKB:B2RHG4}.
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 FimA/Mfa1 family. {ECO:0000305}.
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DR EMBL; AE015924; AAQ65416.1; -; Genomic_DNA.
DR RefSeq; WP_005875055.1; NC_002950.2.
DR PDB; 4RDB; X-ray; 1.45 A; A=30-333.
DR PDBsum; 4RDB; -.
DR AlphaFoldDB; Q7MXK0; -.
DR SMR; Q7MXK0; -.
DR STRING; 242619.PG_0181; -.
DR EnsemblBacteria; AAQ65416; AAQ65416; PG_0181.
DR KEGG; pgi:PG_0181; -.
DR PATRIC; fig|242619.8.peg.168; -.
DR eggNOG; ENOG502ZAWJ; Bacteria.
DR HOGENOM; CLU_833813_0_0_10; -.
DR OMA; GANPAKY; -.
DR OrthoDB; 1465779at2; -.
DR BioCyc; PGIN242619:G1G02-169-MON; -.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; ISS:UniProtKB.
DR InterPro; IPR029141; FimA_N.
DR Pfam; PF06321; P_gingi_FimA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Fimbrium; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal; Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 19..53
FT /evidence="ECO:0000250|UniProtKB:B2RHG4"
FT /id="PRO_0000436798"
FT CHAIN 53..333
FT /note="Minor fimbrium tip subunit MfA4"
FT /id="PRO_0000436799"
FT SITE 53..54
FT /note="Cleavage; by gingipain"
FT /evidence="ECO:0000250|UniProtKB:B2RHG4"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:4RDB"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4RDB"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:4RDB"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:4RDB"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:4RDB"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4RDB"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:4RDB"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 170..190
FT /evidence="ECO:0007829|PDB:4RDB"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 204..216
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:4RDB"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 272..282
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:4RDB"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:4RDB"
FT STRAND 325..333
FT /evidence="ECO:0007829|PDB:4RDB"
SQ SEQUENCE 333 AA; 37139 MW; AD7947D5335BEE33 CRC64;
MKKYLLYASL LTSVLLFSCS KNNPNEPVED RSIEISIRVD DFTKTGEAVR YERNQGSAAE
RLITNLYLLL FDQSGANPAK YYITGNTFTG GTWLPDDMKV KLDMTQSEAG ERKVYVVANV
DNAVKTALDA VANESDLQTV KRTTAMPWST DIASPFLMSG NKTHDFLANR LLDNVPLVRA
IAKVELNISL SEKFQIVPII VNGSLSEFKF RYVNFDKETY VVKPTTKPDN LISSANGVWP
QITDWTVWGA SLNTSPAPDA GTGYTLDANG KVTALRIVTY LNERDSKGAT VEVALPRVDD
GTLPPPEFGP ELYRLPLPDK ILRNHWYKYE VEI
