FIM1F_PARD8
ID FIM1F_PARD8 Reviewed; 318 AA.
AC A6LHQ9;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Putative fimbrium tip subunit Fim1F;
DE Flags: Precursor;
GN OrderedLocusNames=BDI_3522 {ECO:0000312|EMBL:ABR45223.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591 {ECO:0000312|Proteomes:UP000000566};
RN [1] {ECO:0000312|EMBL:ABR45223.1, ECO:0000312|Proteomes:UP000000566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC {ECO:0000312|Proteomes:UP000000566};
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
RN [2]
RP PREDICTED PROPEPTIDE CLEAVAGE.
RX PubMed=26972441; DOI=10.1038/srep22945;
RA Kloppsteck P., Hall M., Hasegawa Y., Persson K.;
RT "Structure of the fimbrial protein Mfa4 from Porphyromonas gingivalis in
RT its precursor form: implications for a donor-strand complementation
RT mechanism.";
RL Sci. Rep. 6:22945-22945(2016).
RN [3] {ECO:0007744|PDB:3R4R}
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 24-318, FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
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: Putative component of the fimbrium tip. Fimbriae are
CC filamentous appendages on the cell surface that mediate cell adhesion
CC and biofilm formation. {ECO:0000305|PubMed:27062925}.
CC -!- SUBUNIT: May be part of the fimbrial tip.
CC {ECO:0000305|PubMed:27062925}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000305|PubMed:27062925}.
CC -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC FimA/Mfa1 family. {ECO:0000305}.
CC -!- CAUTION: A propeptide cleavage site can be predicted based on
CC structural similarity with other family members. Still, this protein
CC lacks the lipidation signal found in other family members, suggesting
CC it may not be exported to the cell surface, and may not be part of the
CC fimbriae. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000140; ABR45223.1; -; Genomic_DNA.
DR RefSeq; WP_009275397.1; NC_009615.1.
DR PDB; 3R4R; X-ray; 2.38 A; A/B=24-318.
DR PDBsum; 3R4R; -.
DR AlphaFoldDB; A6LHQ9; -.
DR SMR; A6LHQ9; -.
DR STRING; 435591.BDI_3522; -.
DR DNASU; 5308671; -.
DR EnsemblBacteria; ABR45223; ABR45223; BDI_3522.
DR KEGG; pdi:BDI_3522; -.
DR HOGENOM; CLU_899122_0_0_10; -.
DR OrthoDB; 2211937at2; -.
DR BioCyc; PDIS435591:G1G5A-3614-MON; -.
DR EvolutionaryTrace; A6LHQ9; -.
DR Proteomes; UP000000566; Chromosome.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR InterPro; IPR029141; FimA_N.
DR Pfam; PF06321; P_gingi_FimA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fimbrium; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..50
FT /evidence="ECO:0000305|PubMed:26972441"
FT /id="PRO_0000436738"
FT CHAIN 51..318
FT /note="Putative fimbrium tip subunit Fim1F"
FT /id="PRO_5002698948"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:3R4R"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 78..87
FT /evidence="ECO:0007829|PDB:3R4R"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 100..112
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3R4R"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:3R4R"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:3R4R"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 188..201
FT /evidence="ECO:0007829|PDB:3R4R"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 270..279
FT /evidence="ECO:0007829|PDB:3R4R"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:3R4R"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:3R4R"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:3R4R"
SQ SEQUENCE 318 AA; 35129 MW; 0E737FCD8BB2F588 CRC64;
MRFNVVLFML IVALLGGLST CSSEVPIGFD TDELSFDMSL VLLTGDMQTK ASDPNYTYAT
TEELTIQNCH VAVFDKDGKR IYFKNFYSKD LGEMKTIGNL SGYELQLEGV RTFGKEDKKV
SVLVVANANN ANNSPFDNLT TYDGVDNSYT AKTIAKGPVT ASLLVKIGKS ETTLKYNQDN
APVTVSLIQL SAKIEYTGVY KKENGELLEG FSLTKVAGLN ASSKITIFNT SAVENGAFSD
LAYPTTKPVT FYTYEISDAF KEVILSVQSG VEPKEYPFPA NKFIKGNYYR IKGLKSSTEI
EWVLENVEDK EVTLDPFE
