FIMH_ECOLI
ID FIMH_ECOLI Reviewed; 300 AA.
AC P08191; Q2M5Z3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Type 1 fimbrin D-mannose specific adhesin;
DE AltName: Full=Protein FimH;
DE Flags: Precursor;
GN Name=fimH; OrderedLocusNames=b4320, JW4283;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
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 [GENOMIC DNA].
RC STRAIN=K12 / CSH-50;
RX PubMed=7905476; DOI=10.1128/jb.176.3.748-755.1994;
RA Sokurenko E.V., Courtney H.S., Ohman D.E., Klemm P., Hasty D.L.;
RT "FimH family of type 1 fimbrial adhesins: functional heterogeneity due to
RT minor sequence variations among fimH genes.";
RL J. Bacteriol. 176:748-755(1994).
RN [3]
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 [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 22-50.
RX PubMed=2900235; DOI=10.1128/jb.170.8.3350-3358.1988;
RA Hanson M.S., Hempel J., Brinton C.C. Jr.;
RT "Purification of the Escherichia coli type 1 pilin and minor pilus proteins
RT and partial characterization of the adhesin protein.";
RL J. Bacteriol. 170:3350-3358(1988).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / PC31;
RX PubMed=1971261; DOI=10.1128/iai.58.6.1995-1998.1990;
RA Krogfelt K.A., Bergmans H., Klemm P.;
RT "Direct evidence that the FimH protein is the mannose-specific adhesin of
RT Escherichia coli type 1 fimbriae.";
RL Infect. Immun. 58:1995-1998(1990).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-300.
RX PubMed=12010488; DOI=10.1046/j.1365-2958.2002.02915.x;
RA Hung C.S., Bouckaert J., Hung D., Pinkner J., Widberg C., DeFusco A.,
RA Auguste C.G., Strouse R., Langermann S., Waksman G., Hultgren S.J.;
RT "Structural basis of tropism of Escherichia coli to the bladder during
RT urinary tract infection.";
RL Mol. Microbiol. 44:903-915(2002).
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 Adhesin responsible for the binding to D-mannose. It is laterally
CC positioned at intervals in the structure of the type 1 fimbriae. In
CC order to integrate FimH in the fimbriae FimF and FimG are needed.
CC {ECO:0000269|PubMed:1971261}.
CC -!- INTERACTION:
CC P08191; P31697: fimC; NbExp=11; IntAct=EBI-1028015, EBI-1028005;
CC P08191; O00322: UPK1A; Xeno; NbExp=2; IntAct=EBI-1028015, EBI-14031976;
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:1971261}.
CC -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR EMBL; X05672; CAA29156.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97216.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77276.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78313.1; -; Genomic_DNA.
DR PIR; S56545; S56545.
DR RefSeq; NP_418740.1; NC_000913.3.
DR RefSeq; WP_000832247.1; NZ_SSUV01000012.1.
DR PDB; 1KIU; X-ray; 3.00 A; B/D/F/H/J/L/N/P=22-300.
DR PDB; 1KLF; X-ray; 2.79 A; B/D/F/H/J/L/N/P=22-300.
DR PDB; 1QUN; X-ray; 2.80 A; B/D/F/H/J/L/N/P=22-300.
DR PDB; 1TR7; X-ray; 2.10 A; A/B=22-179.
DR PDB; 1UWF; X-ray; 1.69 A; A=22-179.
DR PDB; 1ZE3; X-ray; 1.84 A; H=179-300.
DR PDB; 2VCO; X-ray; 2.10 A; A/B=22-179.
DR PDB; 3RFZ; X-ray; 2.80 A; A/D=22-300.
DR PDB; 3ZL1; X-ray; 1.55 A; A/B=22-179.
DR PDB; 3ZL2; X-ray; 1.25 A; A=22-179.
DR PDB; 4ATT; X-ray; 1.25 A; A=22-179.
DR PDB; 4AUJ; X-ray; 1.53 A; A=22-179.
DR PDB; 4AUU; X-ray; 1.60 A; A/B=22-179.
DR PDB; 4AUY; X-ray; 2.10 A; A/B=22-179.
DR PDB; 4AV0; X-ray; 2.10 A; A/B=22-179.
DR PDB; 4AV4; X-ray; 1.90 A; A=22-179.
DR PDB; 4AV5; X-ray; 1.40 A; A/B/C/D=22-179.
DR PDB; 4AVH; X-ray; 2.10 A; A/B=22-179.
DR PDB; 4AVI; X-ray; 2.40 A; A/B=22-179.
DR PDB; 4AVJ; X-ray; 2.10 A; A/B=22-179.
DR PDB; 4AVK; X-ray; 2.40 A; A/B=22-179.
DR PDB; 4CSS; X-ray; 1.07 A; A=22-180.
DR PDB; 4CST; X-ray; 1.10 A; A=22-180.
DR PDB; 4J3O; X-ray; 3.80 A; H=22-300.
DR PDB; 4LOV; X-ray; 1.50 A; A=22-179.
DR PDB; 4X50; X-ray; 2.00 A; A/B=22-180.
DR PDB; 4X5P; X-ray; 1.00 A; A=22-180.
DR PDB; 4X5Q; X-ray; 1.12 A; A=22-180.
DR PDB; 4X5R; X-ray; 1.65 A; A/B/C=22-180.
DR PDB; 4XO8; X-ray; 1.70 A; A/B=22-179.
DR PDB; 4XO9; X-ray; 1.14 A; A=22-300.
DR PDB; 4XOA; X-ray; 2.54 A; A/C/E/G=22-300.
DR PDB; 4XOB; X-ray; 3.00 A; A/C/E/G=22-300.
DR PDB; 4XOD; X-ray; 1.14 A; A=22-300.
DR PDB; 5ABZ; X-ray; 2.40 A; A/B=22-179.
DR PDB; 5CGB; X-ray; 1.60 A; A/B=22-179.
DR PDB; 5F2F; X-ray; 1.67 A; A=22-179.
DR PDB; 5F3F; X-ray; 1.76 A; A=22-179.
DR PDB; 5FS5; X-ray; 1.42 A; A=22-179.
DR PDB; 5FWR; X-ray; 2.13 A; A/B/C/D/E/F/G/H=22-179.
DR PDB; 5FX3; X-ray; 1.90 A; A=22-179.
DR PDB; 5JCQ; X-ray; 1.60 A; A/B=22-179.
DR PDB; 5JCR; X-ray; 1.70 A; A/B=22-179.
DR PDB; 5L4T; X-ray; 1.90 A; A/B=22-179.
DR PDB; 5L4U; X-ray; 2.10 A; A/B=22-179.
DR PDB; 5L4V; X-ray; 2.99 A; A/B/C=22-179.
DR PDB; 5L4W; X-ray; 1.90 A; A/B/C=22-179.
DR PDB; 5L4X; X-ray; 1.90 A; A/B=22-179.
DR PDB; 5L4Y; X-ray; 1.90 A; A/B=22-179.
DR PDB; 5MCA; X-ray; 1.60 A; A=22-180.
DR PDB; 5MTS; X-ray; 2.60 A; A/B=1-300.
DR PDB; 5MUC; X-ray; 2.60 A; A/B=22-179.
DR PDB; 6E14; EM; 4.00 A; H=1-300.
DR PDB; 6E15; EM; 6.20 A; H=1-300.
DR PDB; 6G2R; X-ray; 2.10 A; A/B=22-179.
DR PDB; 6G2S; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I=22-179.
DR PDB; 6GTX; X-ray; 2.50 A; A/B/C/D=22-179.
DR PDB; 6GTY; X-ray; 1.90 A; A/B/C/D/E=22-179.
DR PDB; 6YHW; X-ray; 1.96 A; A/B=1-300.
DR PDB; 7AYN; X-ray; 1.42 A; A/B/C/D=22-179.
DR PDBsum; 1KIU; -.
DR PDBsum; 1KLF; -.
DR PDBsum; 1QUN; -.
DR PDBsum; 1TR7; -.
DR PDBsum; 1UWF; -.
DR PDBsum; 1ZE3; -.
DR PDBsum; 2VCO; -.
DR PDBsum; 3RFZ; -.
DR PDBsum; 3ZL1; -.
DR PDBsum; 3ZL2; -.
DR PDBsum; 4ATT; -.
DR PDBsum; 4AUJ; -.
DR PDBsum; 4AUU; -.
DR PDBsum; 4AUY; -.
DR PDBsum; 4AV0; -.
DR PDBsum; 4AV4; -.
DR PDBsum; 4AV5; -.
DR PDBsum; 4AVH; -.
DR PDBsum; 4AVI; -.
DR PDBsum; 4AVJ; -.
DR PDBsum; 4AVK; -.
DR PDBsum; 4CSS; -.
DR PDBsum; 4CST; -.
DR PDBsum; 4J3O; -.
DR PDBsum; 4LOV; -.
DR PDBsum; 4X50; -.
DR PDBsum; 4X5P; -.
DR PDBsum; 4X5Q; -.
DR PDBsum; 4X5R; -.
DR PDBsum; 4XO8; -.
DR PDBsum; 4XO9; -.
DR PDBsum; 4XOA; -.
DR PDBsum; 4XOB; -.
DR PDBsum; 4XOD; -.
DR PDBsum; 5ABZ; -.
DR PDBsum; 5CGB; -.
DR PDBsum; 5F2F; -.
DR PDBsum; 5F3F; -.
DR PDBsum; 5FS5; -.
DR PDBsum; 5FWR; -.
DR PDBsum; 5FX3; -.
DR PDBsum; 5JCQ; -.
DR PDBsum; 5JCR; -.
DR PDBsum; 5L4T; -.
DR PDBsum; 5L4U; -.
DR PDBsum; 5L4V; -.
DR PDBsum; 5L4W; -.
DR PDBsum; 5L4X; -.
DR PDBsum; 5L4Y; -.
DR PDBsum; 5MCA; -.
DR PDBsum; 5MTS; -.
DR PDBsum; 5MUC; -.
DR PDBsum; 6E14; -.
DR PDBsum; 6E15; -.
DR PDBsum; 6G2R; -.
DR PDBsum; 6G2S; -.
DR PDBsum; 6GTX; -.
DR PDBsum; 6GTY; -.
DR PDBsum; 6YHW; -.
DR PDBsum; 7AYN; -.
DR AlphaFoldDB; P08191; -.
DR BMRB; P08191; -.
DR SMR; P08191; -.
DR BioGRID; 4262737; 8.
DR ComplexPortal; CPX-2855; Fimbrial Tip Complex FimFGH.
DR DIP; DIP-9616N; -.
DR IntAct; P08191; 3.
DR STRING; 511145.b4320; -.
DR BindingDB; P08191; -.
DR ChEMBL; CHEMBL4837; -.
DR UniLectin; P08191; -.
DR PaxDb; P08191; -.
DR PRIDE; P08191; -.
DR EnsemblBacteria; AAC77276; AAC77276; b4320.
DR EnsemblBacteria; BAE78313; BAE78313; BAE78313.
DR GeneID; 948847; -.
DR KEGG; ecj:JW4283; -.
DR KEGG; eco:b4320; -.
DR PATRIC; fig|1411691.4.peg.2372; -.
DR EchoBASE; EB0311; -.
DR eggNOG; COG3539; Bacteria.
DR HOGENOM; CLU_080390_0_0_6; -.
DR OMA; FIWNIYA; -.
DR BioCyc; EcoCyc:EG10315-MON; -.
DR EvolutionaryTrace; P08191; -.
DR PHI-base; PHI:2690; -.
DR PHI-base; PHI:7180; -.
DR PHI-base; PHI:7204; -.
DR PHI-base; PHI:7846; -.
DR PHI-base; PHI:8107; -.
DR PRO; PR:P08191; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0033644; C:host cell membrane; IDA:UniProtKB.
DR GO; GO:0009289; C:pilus; IMP:EcoCyc.
DR GO; GO:0009419; C:pilus tip; IPI:ComplexPortal.
DR GO; GO:0005537; F:mannose binding; IDA:EcoCyc.
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 CDD; cd10466; FimH_man-bind; 1.
DR Gene3D; 2.60.40.1090; -; 2.
DR InterPro; IPR000259; Adhesion_dom_fimbrial.
DR InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR015243; FimH_man-bd.
DR Pfam; PF00419; Fimbrial; 1.
DR Pfam; PF09160; FimH_man-bind; 1.
DR SUPFAM; SSF49401; SSF49401; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Fimbrium; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2900235"
FT CHAIN 22..300
FT /note="Type 1 fimbrin D-mannose specific adhesin"
FT /id="PRO_0000009211"
FT CONFLICT 79
FT /note="L -> R (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="P -> R (in Ref. 1; CAA29156)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="T -> H (in Ref. 1; CAA29156 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4XOD"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:4X5P"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:4X5P"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:4X5P"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4XO9"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4XO9"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 146..159
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 163..173
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:4X5P"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:4XO9"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:4XO9"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1ZE3"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1KLF"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4XO9"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:4XO9"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:4XOA"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:4XO9"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:4XO9"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:4XO9"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:4XO9"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:1KLF"
FT STRAND 286..299
FT /evidence="ECO:0007829|PDB:4XO9"
SQ SEQUENCE 300 AA; 31473 MW; 939204A51658747D CRC64;
MKRVITLFAV LLMGWSVNAW SFACKTANGT AIPIGGGSAN VYVNLAPVVN VGQNLVVDLS
TQIFCHNDYP ETITDYVTLQ RGSAYGGVLS NFSGTVKYSG SSYPFPTTSE TPRVVYNSRT
DKPWPVALYL TPVSSAGGVA IKAGSLIAVL ILRQTNNYNS DDFQFVWNIY ANNDVVVPTG
GCDVSARDVT VTLPDYPGSV PIPLTVYCAK SQNLGYYLSG TTADAGNSIF TNTASFSPAQ
GVGVQLTRNG TIIPANNTVS LGAVGTSAVS LGLTANYART GGQVTAGNVQ SIIGVTFVYQ
