FIM1C_PHOV8
ID FIM1C_PHOV8 Reviewed; 379 AA.
AC A6L3B5;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Fimbrium subunit Fim1C;
DE Flags: Precursor;
GN Name=fim1C; OrderedLocusNames=BVU_2522 {ECO:0000312|EMBL:ABR40179.1};
OS Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Phocaeicola.
OX NCBI_TaxID=435590 {ECO:0000312|Proteomes:UP000002861};
RN [1] {ECO:0000312|EMBL:ABR40179.1, ECO:0000312|Proteomes:UP000002861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC 11154 {ECO:0000312|Proteomes:UP000002861};
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 X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 22-379, FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC 11154 {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: 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. Mfa-
CC like family. {ECO:0000305}.
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DR EMBL; CP000139; ABR40179.1; -; Genomic_DNA.
DR RefSeq; WP_005847458.1; NC_009614.1.
DR PDB; 4QB7; X-ray; 2.55 A; A=22-379.
DR PDBsum; 4QB7; -.
DR AlphaFoldDB; A6L3B5; -.
DR SMR; A6L3B5; -.
DR STRING; 435590.BVU_2522; -.
DR DNASU; 5303486; -.
DR EnsemblBacteria; ABR40179; ABR40179; BVU_2522.
DR KEGG; bvu:BVU_2522; -.
DR eggNOG; ENOG5033U1D; Bacteria.
DR HOGENOM; CLU_042631_0_0_10; -.
DR OMA; AYAPYES; -.
DR OrthoDB; 1626312at2; -.
DR BioCyc; BVUL435590:G1G59-2626-MON; -.
DR Proteomes; UP000002861; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.2620; -; 1.
DR InterPro; IPR025049; Mfa-like_1.
DR InterPro; IPR042278; Mfa-like_1_N.
DR Pfam; PF13149; Mfa_like_1; 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..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT PROPEP 18..45
FT /evidence="ECO:0000255"
FT /id="PRO_0000436736"
FT CHAIN 46..379
FT /note="Fimbrium subunit Fim1C"
FT /id="PRO_0000436737"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:4QB7"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:4QB7"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:4QB7"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:4QB7"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:4QB7"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:4QB7"
FT TURN 151..156
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4QB7"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:4QB7"
FT TURN 173..178
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 188..200
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 204..216
FT /evidence="ECO:0007829|PDB:4QB7"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:4QB7"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4QB7"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:4QB7"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 304..318
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 321..333
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 343..351
FT /evidence="ECO:0007829|PDB:4QB7"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:4QB7"
SQ SEQUENCE 379 AA; 42244 MW; 795BE57E2326140C CRC64;
MEVKSLLMVM ATLTIAGCSQ NEMTEMNPDT NRTIGLDVYT EVQTRGTETT TSTLKANAGF
GIFAYQTSSA GWNSEKGNTT PNFMYNEHAT WTSDSWGYTN LRFWPIDDKK ITFFAYAPYE
SKPEVGTDQK ITLSGQNAKG APTITFEVKT SNNWKDMIDL VTDCHTAIQD QTNESNKGTV
QFKFSHVLTQ IANIKVKPDV NLGTDTKIFV TGLKLDPGST TLYNKAVYKF DNDTWEAISP
DASYFSTEQD LSDFLNKTTT DQWGYNKSSI NVSDDQNATA LFSDTEALYF IPVNNKNGTT
NAGDLKLKIN YDIVTKVTDT SNLTSTITNK EVSLPKNTFK KGTKHTYVLT IKMNAIKITV
EDNMEGWTDD SDSDINVEK
