FIMF_ECOLI
ID FIMF_ECOLI Reviewed; 176 AA.
AC P08189; Q2M5Z5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein FimF;
DE Flags: Precursor;
GN Name=fimF; OrderedLocusNames=b4318, JW4281;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2890081; DOI=10.1007/bf00328136;
RA Klemm P., Christiansen G.;
RT "Three fim genes required for the regulation of length and mediation of
RT adhesion of Escherichia coli type 1 fimbriae.";
RL Mol. Gen. Genet. 208:439-445(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
RC STRAIN=K12;
RX PubMed=1970114; DOI=10.1007/bf00260505;
RA Klemm P., Christiansen G.;
RT "The fimD gene required for cell surface localization of Escherichia coli
RT type 1 fimbriae.";
RL Mol. Gen. Genet. 220:334-338(1990).
CC -!- FUNCTION: Involved in regulation of length and mediation of adhesion of
CC type 1 fimbriae (but not necessary for the production of fimbriae).
CC Involved in the integration of FimH in the fimbriae.
CC -!- SUBCELLULAR LOCATION: Fimbrium.
CC -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR EMBL; X05672; CAA29154.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97214.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77274.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78311.1; -; Genomic_DNA.
DR EMBL; X51655; CAA35969.1; -; Genomic_DNA.
DR PIR; S56543; S56543.
DR RefSeq; NP_418738.1; NC_000913.3.
DR RefSeq; WP_001244827.1; NZ_SSUV01000012.1.
DR PDB; 2JMR; NMR; -; A=23-176.
DR PDB; 3BFQ; X-ray; 1.34 A; F=23-37.
DR PDB; 3BFW; X-ray; 1.80 A; B/D=23-37.
DR PDB; 3BWU; X-ray; 1.76 A; F=35-176.
DR PDB; 3JWN; X-ray; 2.69 A; E/F/K/L=23-176.
DR PDB; 4J3O; X-ray; 3.80 A; F=23-176.
DR PDB; 4XOB; X-ray; 3.00 A; B/D/F/H=23-37.
DR PDB; 5IQM; X-ray; 1.50 A; B/F=23-37.
DR PDB; 5IQN; X-ray; 1.00 A; B/F=25-34.
DR PDB; 5IQO; X-ray; 1.30 A; B/D=23-37.
DR PDB; 6E14; EM; 4.00 A; F=21-176.
DR PDB; 6E15; EM; 6.20 A; F=21-176.
DR PDBsum; 2JMR; -.
DR PDBsum; 3BFQ; -.
DR PDBsum; 3BFW; -.
DR PDBsum; 3BWU; -.
DR PDBsum; 3JWN; -.
DR PDBsum; 4J3O; -.
DR PDBsum; 4XOB; -.
DR PDBsum; 5IQM; -.
DR PDBsum; 5IQN; -.
DR PDBsum; 5IQO; -.
DR PDBsum; 6E14; -.
DR PDBsum; 6E15; -.
DR AlphaFoldDB; P08189; -.
DR BMRB; P08189; -.
DR SMR; P08189; -.
DR BioGRID; 4262749; 4.
DR ComplexPortal; CPX-2855; Fimbrial Tip Complex FimFGH.
DR DIP; DIP-9614N; -.
DR IntAct; P08189; 1.
DR MINT; P08189; -.
DR STRING; 511145.b4318; -.
DR PaxDb; P08189; -.
DR PRIDE; P08189; -.
DR EnsemblBacteria; AAC77274; AAC77274; b4318.
DR EnsemblBacteria; BAE78311; BAE78311; BAE78311.
DR GeneID; 948845; -.
DR KEGG; ecj:JW4281; -.
DR KEGG; eco:b4318; -.
DR PATRIC; fig|1411691.4.peg.2374; -.
DR EchoBASE; EB0309; -.
DR eggNOG; COG3539; Bacteria.
DR HOGENOM; CLU_088965_0_2_6; -.
DR InParanoid; P08189; -.
DR OMA; YVRDNAC; -.
DR PhylomeDB; P08189; -.
DR BioCyc; EcoCyc:EG10313-MON; -.
DR EvolutionaryTrace; P08189; -.
DR PRO; PR:P08189; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009289; C:pilus; IBA:GO_Central.
DR GO; GO:0009419; C:pilus tip; IPI:ComplexPortal.
DR GO; GO:0007155; P:cell adhesion; IMP:ComplexPortal.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:ComplexPortal.
DR GO; GO:0007638; P:mechanosensory behavior; IDA:ComplexPortal.
DR Gene3D; 2.60.40.1090; -; 1.
DR InterPro; IPR000259; Adhesion_dom_fimbrial.
DR InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR Pfam; PF00419; Fimbrial; 1.
DR SUPFAM; SSF49401; SSF49401; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Fimbrium; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..176
FT /note="Protein FimF"
FT /id="PRO_0000009207"
FT SITE 175
FT /note="Required for stability and transport"
FT /evidence="ECO:0000250"
FT DISULFID 38..78
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="P -> S (in Ref. 1; CAA29154)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="S -> L (in Ref. 1; CAA29154)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="A -> V (in Ref. 1; CAA29154)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..92
FT /note="AVKVGFTGV -> RRKGWVYWR (in Ref. 1; CAA29154)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="V -> A (in Ref. 1; CAA29154)"
FT /evidence="ECO:0000305"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:5IQN"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2JMR"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3BWU"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2JMR"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:3JWN"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2JMR"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:3BWU"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3BWU"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3BWU"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3JWN"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:3BWU"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2JMR"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3BWU"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3BWU"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3JWN"
FT STRAND 145..159
FT /evidence="ECO:0007829|PDB:3BWU"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:3BWU"
SQ SEQUENCE 176 AA; 18715 MW; 38692EFE6A40121F CRC64;
MRNKPFYLLC AFLWLAVSHA LAADSTITIR GYVRDNGCSV AAESTNFTVD LMENAAKQFN
NIGATTPVVP FRILLSPCGN AVSAVKVGFT GVADSHNANL LALENTVSAA SGLGIQLLNE
QQNQIPLNAP SSALSWTTLT PGKPNTLNFY ARLMATQVPV TAGHINATAT FTLEYQ
