FIM1C_PARD8
ID FIM1C_PARD8 Reviewed; 375 AA.
AC A6LHQ6;
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 Fim1C;
DE Flags: Precursor;
GN OrderedLocusNames=BDI_3519 {ECO:0000312|EMBL:ABR45220.1};
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:ABR45220.1, 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:4JG5}
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 22-375, FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
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: Probably a 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}. 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. Probably part of the
CC fimbrium tip. {ECO:0000305|PubMed:27062925}.
CC -!- SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily.
CC FimA/Mfa1 family. {ECO:0000305}.
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DR EMBL; CP000140; ABR45220.1; -; Genomic_DNA.
DR RefSeq; WP_009016908.1; NC_009615.1.
DR PDB; 4JG5; X-ray; 2.34 A; A=22-375.
DR PDBsum; 4JG5; -.
DR AlphaFoldDB; A6LHQ6; -.
DR SMR; A6LHQ6; -.
DR STRING; 435591.BDI_3519; -.
DR DNASU; 5308668; -.
DR EnsemblBacteria; ABR45220; ABR45220; BDI_3519.
DR KEGG; pdi:BDI_3519; -.
DR HOGENOM; CLU_741558_0_0_10; -.
DR OrthoDB; 1408699at2; -.
DR BioCyc; PDIS435591:G1G5A-3611-MON; -.
DR Proteomes; UP000000566; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
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.
FT SIGNAL 1..16
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 17..47
FT /evidence="ECO:0000305|PubMed:26972441"
FT /id="PRO_0000436733"
FT CHAIN 48..375
FT /note="Putative fimbrium tip subunit Fim1C"
FT /id="PRO_0000436734"
FT LIPID 17
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 17
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4JG5"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:4JG5"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:4JG5"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4JG5"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4JG5"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4JG5"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:4JG5"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:4JG5"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 180..197
FT /evidence="ECO:0007829|PDB:4JG5"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 208..218
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:4JG5"
FT TURN 302..310
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 320..329
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:4JG5"
FT STRAND 357..364
FT /evidence="ECO:0007829|PDB:4JG5"
SQ SEQUENCE 375 AA; 41000 MW; D864EA25F2B160C6 CRC64;
MKLLANIFLS GLAILACVSC SKDEDPVLPL EGAKLSVAVK ASGTATKAYN PNDVNELEGE
AYINNLAVVV FNETGTELLG YKWEALSGAE HSAIIADVPT TKAVRARIIV LANVPRDLLS
TVSTYDEFQT RLVDLSSQSQ TNLTMSSQVI VTKSALSEED NYLGYTDLGD QNVDGISDPI
LLTRVAARID LVNISTRFAG TPFAGREVRI DAVGIYNMKT KSYYFSEADW GETEAPDAVR
NSEDTSFEDL LVNDGTSISN TPFVHYVMEN MKSDDHTMIA VKATLRGNSS YQDHTKIFTA
VINAGGLQNG YDHNFIRRNY VYRLRIYFDG ESFDNIPVTP DPGPGPDPEP EVDTNLNIAV
QVVGWGPVMQ HPVID
