UniProtKB - P08191 (FIMH_ECOLI)
Protein
Type 1 fimbrin D-mannose specific adhesin
Gene
fimH
Organism
Escherichia coli (strain K12)
Status
Functioni
Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.1 Publication
GO - Molecular functioni
- mannose binding Source: EcoCyc
GO - Biological processi
- cell adhesion Source: EcoCyc
- cell adhesion involved in single-species biofilm formation Source: GO_Central
- pilus organization Source: GO_Central
Enzyme and pathway databases
BioCyci | EcoCyc:EG10315-MONOMER |
Protein family/group databases
UniLectini | P08191 |
Names & Taxonomyi
Protein namesi | Recommended name: Type 1 fimbrin D-mannose specific adhesinAlternative name(s): Protein FimH |
Gene namesi | Name:fimH Ordered Locus Names:b4320, JW4283 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Other locations
- Fimbrium 1 Publication
Other locations
- host cell membrane Source: UniProtKB
- pilus Source: EcoCyc
Keywords - Cellular componenti
FimbriumPathology & Biotechi
Miscellaneous databases
PHI-basei | PHI:2690 PHI:7180 PHI:7204 PHI:7846 PHI:8107 |
Chemistry databases
ChEMBLi | CHEMBL4837 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 21 | 1 PublicationAdd BLAST | 21 | |
ChainiPRO_0000009211 | 22 – 300 | Type 1 fimbrin D-mannose specific adhesinAdd BLAST | 279 |
Proteomic databases
PaxDbi | P08191 |
PRIDEi | P08191 |
Interactioni
Binary interactionsi
Hide detailsP08191
With | #Exp. | IntAct |
---|---|---|
fimC [P31697] | 11 | EBI-1028015,EBI-1028005 |
UPK1A [O00322] from Homo sapiens. | 2 | EBI-1028015,EBI-14031976 |
Protein-protein interaction databases
BioGRIDi | 4262737, 8 interactors |
ComplexPortali | CPX-2855, Fimbrial Tip Complex FimFGH |
DIPi | DIP-9616N |
IntActi | P08191, 3 interactors |
STRINGi | 511145.b4320 |
Chemistry databases
BindingDBi | P08191 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | P08191 |
SMRi | P08191 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P08191 |
Family & Domainsi
Sequence similaritiesi
Belongs to the fimbrial protein family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | COG3539, Bacteria |
HOGENOMi | CLU_080390_0_0_6 |
Family and domain databases
CDDi | cd10466, FimH_man-bind, 1 hit |
Gene3Di | 2.60.40.1090, 2 hits |
InterProi | View protein in InterPro IPR000259, Adhesion_dom_fimbrial IPR036937, Adhesion_dom_fimbrial_sf IPR008966, Adhesion_dom_sf IPR015243, FimH_man-bd |
Pfami | View protein in Pfam PF00419, Fimbrial, 1 hit PF09160, FimH_man-bind, 1 hit |
SUPFAMi | SSF49401, SSF49401, 2 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P08191-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKRVITLFAV LLMGWSVNAW SFACKTANGT AIPIGGGSAN VYVNLAPVVN
60 70 80 90 100
VGQNLVVDLS TQIFCHNDYP ETITDYVTLQ RGSAYGGVLS NFSGTVKYSG
110 120 130 140 150
SSYPFPTTSE TPRVVYNSRT DKPWPVALYL TPVSSAGGVA IKAGSLIAVL
160 170 180 190 200
ILRQTNNYNS DDFQFVWNIY ANNDVVVPTG GCDVSARDVT VTLPDYPGSV
210 220 230 240 250
PIPLTVYCAK SQNLGYYLSG TTADAGNSIF TNTASFSPAQ GVGVQLTRNG
260 270 280 290 300
TIIPANNTVS LGAVGTSAVS LGLTANYART GGQVTAGNVQ SIIGVTFVYQ
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 79 | L → R no nucleotide entry (PubMed:7905476).Curated | 1 | |
Sequence conflicti | 197 | P → R in CAA29156 (PubMed:2890081).Curated | 1 | |
Sequence conflicti | 222 | T → H in CAA29156 (PubMed:2890081).Curated | 1 | |
Sequence conflicti | 222 | T → H no nucleotide entry (PubMed:7905476).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X05672 Genomic DNA Translation: CAA29156.1 U14003 Genomic DNA Translation: AAA97216.1 U00096 Genomic DNA Translation: AAC77276.1 AP009048 Genomic DNA Translation: BAE78313.1 |
PIRi | S56545 |
RefSeqi | NP_418740.1, NC_000913.3 WP_000832247.1, NZ_SSUV01000012.1 |
Genome annotation databases
EnsemblBacteriai | AAC77276; AAC77276; b4320 BAE78313; BAE78313; BAE78313 |
GeneIDi | 948847 |
KEGGi | ecj:JW4283 eco:b4320 |
PATRICi | fig|1411691.4.peg.2372 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X05672 Genomic DNA Translation: CAA29156.1 U14003 Genomic DNA Translation: AAA97216.1 U00096 Genomic DNA Translation: AAC77276.1 AP009048 Genomic DNA Translation: BAE78313.1 |
PIRi | S56545 |
RefSeqi | NP_418740.1, NC_000913.3 WP_000832247.1, NZ_SSUV01000012.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1KIU | X-ray | 3.00 | B/D/F/H/J/L/N/P | 22-300 | [»] | |
1KLF | X-ray | 2.79 | B/D/F/H/J/L/N/P | 22-300 | [»] | |
1QUN | X-ray | 2.80 | B/D/F/H/J/L/N/P | 22-300 | [»] | |
1TR7 | X-ray | 2.10 | A/B | 22-179 | [»] | |
1UWF | X-ray | 1.69 | A | 22-179 | [»] | |
1ZE3 | X-ray | 1.84 | H | 179-300 | [»] | |
2VCO | X-ray | 2.10 | A/B | 22-179 | [»] | |
3RFZ | X-ray | 2.80 | A/D | 22-300 | [»] | |
3ZL1 | X-ray | 1.55 | A/B | 22-179 | [»] | |
3ZL2 | X-ray | 1.25 | A | 22-179 | [»] | |
4ATT | X-ray | 1.25 | A | 22-179 | [»] | |
4AUJ | X-ray | 1.53 | A | 22-179 | [»] | |
4AUU | X-ray | 1.60 | A/B | 22-179 | [»] | |
4AUY | X-ray | 2.10 | A/B | 22-179 | [»] | |
4AV0 | X-ray | 2.10 | A/B | 22-179 | [»] | |
4AV4 | X-ray | 1.90 | A | 22-179 | [»] | |
4AV5 | X-ray | 1.40 | A/B/C/D | 22-179 | [»] | |
4AVH | X-ray | 2.10 | A/B | 22-179 | [»] | |
4AVI | X-ray | 2.40 | A/B | 22-179 | [»] | |
4AVJ | X-ray | 2.10 | A/B | 22-179 | [»] | |
4AVK | X-ray | 2.40 | A/B | 22-179 | [»] | |
4CSS | X-ray | 1.07 | A | 22-180 | [»] | |
4CST | X-ray | 1.10 | A | 22-180 | [»] | |
4J3O | X-ray | 3.80 | H | 22-300 | [»] | |
4LOV | X-ray | 1.50 | A | 22-179 | [»] | |
4X50 | X-ray | 2.00 | A/B | 22-180 | [»] | |
4X5P | X-ray | 1.00 | A | 22-180 | [»] | |
4X5Q | X-ray | 1.12 | A | 22-180 | [»] | |
4X5R | X-ray | 1.65 | A/B/C | 22-180 | [»] | |
4XO8 | X-ray | 1.70 | A/B | 22-179 | [»] | |
4XO9 | X-ray | 1.14 | A | 22-300 | [»] | |
4XOA | X-ray | 2.54 | A/C/E/G | 22-300 | [»] | |
4XOB | X-ray | 3.00 | A/C/E/G | 22-300 | [»] | |
4XOD | X-ray | 1.14 | A | 22-300 | [»] | |
5ABZ | X-ray | 2.40 | A/B | 22-179 | [»] | |
5CGB | X-ray | 1.60 | A/B | 22-179 | [»] | |
5F2F | X-ray | 1.67 | A | 22-179 | [»] | |
5F3F | X-ray | 1.76 | A | 22-179 | [»] | |
5FS5 | X-ray | 1.42 | A | 22-179 | [»] | |
5FWR | X-ray | 2.13 | A/B/C/D/E/F/G/H | 22-179 | [»] | |
5FX3 | X-ray | 1.90 | A | 22-179 | [»] | |
5JCQ | X-ray | 1.60 | A/B | 22-179 | [»] | |
5JCR | X-ray | 1.70 | A/B | 22-179 | [»] | |
5L4T | X-ray | 1.90 | A/B | 22-179 | [»] | |
5L4U | X-ray | 2.10 | A/B | 22-179 | [»] | |
5L4V | X-ray | 2.99 | A/B/C | 22-179 | [»] | |
5L4W | X-ray | 1.90 | A/B/C | 22-179 | [»] | |
5L4X | X-ray | 1.90 | A/B | 22-179 | [»] | |
5L4Y | X-ray | 1.90 | A/B | 22-179 | [»] | |
5MCA | X-ray | 1.60 | A | 22-180 | [»] | |
5MTS | X-ray | 2.60 | A/B | 1-300 | [»] | |
5MUC | X-ray | 2.60 | A/B | 22-179 | [»] | |
6E14 | electron microscopy | 4.00 | H | 1-300 | [»] | |
6E15 | electron microscopy | 6.20 | H | 1-300 | [»] | |
6G2R | X-ray | 2.10 | A/B | 22-179 | [»] | |
6G2S | X-ray | 2.20 | A/B/C/D/E/F/G/H/I | 22-179 | [»] | |
6GTX | X-ray | 2.50 | A/B/C/D | 22-179 | [»] | |
6GTY | X-ray | 1.90 | A/B/C/D/E | 22-179 | [»] | |
6YHW | X-ray | 1.96 | A/B | 1-300 | [»] | |
7AYN | X-ray | 1.42 | A/B/C/D | 22-179 | [»] | |
BMRBi | P08191 | |||||
SMRi | P08191 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262737, 8 interactors |
ComplexPortali | CPX-2855, Fimbrial Tip Complex FimFGH |
DIPi | DIP-9616N |
IntActi | P08191, 3 interactors |
STRINGi | 511145.b4320 |
Chemistry databases
BindingDBi | P08191 |
ChEMBLi | CHEMBL4837 |
Protein family/group databases
UniLectini | P08191 |
Proteomic databases
PaxDbi | P08191 |
PRIDEi | P08191 |
Genome annotation databases
EnsemblBacteriai | AAC77276; AAC77276; b4320 BAE78313; BAE78313; BAE78313 |
GeneIDi | 948847 |
KEGGi | ecj:JW4283 eco:b4320 |
PATRICi | fig|1411691.4.peg.2372 |
Organism-specific databases
EchoBASEi | EB0311 |
Phylogenomic databases
eggNOGi | COG3539, Bacteria |
HOGENOMi | CLU_080390_0_0_6 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10315-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P08191 |
PHI-basei | PHI:2690 PHI:7180 PHI:7204 PHI:7846 PHI:8107 |
PROi | PR:P08191 |
Family and domain databases
CDDi | cd10466, FimH_man-bind, 1 hit |
Gene3Di | 2.60.40.1090, 2 hits |
InterProi | View protein in InterPro IPR000259, Adhesion_dom_fimbrial IPR036937, Adhesion_dom_fimbrial_sf IPR008966, Adhesion_dom_sf IPR015243, FimH_man-bd |
Pfami | View protein in Pfam PF00419, Fimbrial, 1 hit PF09160, FimH_man-bind, 1 hit |
SUPFAMi | SSF49401, SSF49401, 2 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FIMH_ECOLI | |
Accessioni | P08191Primary (citable) accession number: P08191 Secondary accession number(s): Q2M5Z3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
Last sequence update: | February 1, 1995 | |
Last modified: | April 7, 2021 | |
This is version 175 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families