Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein FimH

Gene

fimH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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.

GO - Molecular functioni

  • mannose binding Source: EcoCyc

GO - Biological processi

  • cell adhesion Source: EcoCyc
Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:EG10315-MONOMER.
ECOL316407:JW4283-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein FimH
Gene namesi
Name:fimH
Ordered Locus Names:b4320, JW4283
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10315. fimH.

Subcellular locationi

GO - Cellular componenti

  • pilus Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Fimbrium

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4837.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 300279Protein FimHPRO_0000009211Add
BLAST

Proteomic databases

PaxDbiP08191.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
fimCP316976EBI-1028015,EBI-1028005

Protein-protein interaction databases

BioGridi4262737. 8 interactions.
DIPiDIP-9616N.
IntActiP08191. 2 interactions.
STRINGi511145.b4320.

Chemistry

BindingDBiP08191.

Structurei

Secondary structure

1
300
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 264Combined sources
Beta strandi37 – 437Combined sources
Beta strandi48 – 503Combined sources
Beta strandi55 – 584Combined sources
Helixi59 – 613Combined sources
Beta strandi63 – 664Combined sources
Turni70 – 723Combined sources
Beta strandi75 – 8410Combined sources
Helixi86 – 916Combined sources
Beta strandi92 – 987Combined sources
Beta strandi101 – 1066Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi126 – 1327Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi138 – 1414Combined sources
Beta strandi146 – 15914Combined sources
Beta strandi163 – 17311Combined sources
Beta strandi175 – 1773Combined sources
Beta strandi180 – 1856Combined sources
Beta strandi187 – 1926Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi205 – 2106Combined sources
Beta strandi212 – 2209Combined sources
Beta strandi222 – 2243Combined sources
Beta strandi235 – 2384Combined sources
Beta strandi240 – 2489Combined sources
Beta strandi259 – 2646Combined sources
Beta strandi273 – 2797Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi286 – 29914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KIUX-ray3.00B/D/F/H/J/L/N/P22-300[»]
1KLFX-ray2.79B/D/F/H/J/L/N/P22-300[»]
1QUNX-ray2.80B/D/F/H/J/L/N/P22-300[»]
1TR7X-ray2.10A/B22-179[»]
1UWFX-ray1.69A22-179[»]
1ZE3X-ray1.84H179-300[»]
2VCOX-ray2.10A/B22-179[»]
3RFZX-ray2.80A/D22-300[»]
3ZL1X-ray1.55A/B22-179[»]
3ZL2X-ray1.25A22-179[»]
4ATTX-ray1.25A22-179[»]
4AUJX-ray1.53A22-179[»]
4AUUX-ray1.60A/B22-179[»]
4AUYX-ray2.10A/B22-179[»]
4AV0X-ray2.10A/B22-179[»]
4AV4X-ray1.90A22-179[»]
4AV5X-ray1.40A/B/C/D22-179[»]
4AVHX-ray2.10A/B22-179[»]
4AVIX-ray2.40A/B22-179[»]
4AVJX-ray2.10A/B22-179[»]
4AVKX-ray2.40A/B22-179[»]
4CSSX-ray1.07A22-180[»]
4CSTX-ray1.10A22-180[»]
4J3OX-ray3.80H22-300[»]
4LOVX-ray1.50A22-179[»]
4X50X-ray2.00A/B22-180[»]
4X5PX-ray1.00A22-180[»]
4X5QX-ray1.12A22-180[»]
4X5RX-ray1.65A/B/C22-180[»]
4XO8X-ray1.70A/B22-179[»]
4XO9X-ray1.14A22-300[»]
4XOAX-ray2.54A/C/E/G22-300[»]
4XOBX-ray3.00A/C/E/G22-300[»]
4XODX-ray1.14A22-300[»]
5AB1X-ray1.96A/B1-300[»]
5ABZX-ray2.40A/B22-179[»]
5F2FX-ray1.67A22-179[»]
ProteinModelPortaliP08191.
SMRiP08191. Positions 22-300.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08191.

Family & Domainsi

Sequence similaritiesi

Belongs to the fimbrial protein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410643X. Bacteria.
ENOG410Y3E1. LUCA.
HOGENOMiHOG000120719.
KOiK07350.
OMAiDYPGSMA.

Family and domain databases

CDDicd10466. FimH_man-bind. 1 hit.
Gene3Di2.60.40.1090. 2 hits.
InterProiIPR008966. Adhesion_dom.
IPR000259. Adhesion_dom_fimbrial.
IPR015243. FimH_man-bd.
[Graphical view]
PfamiPF00419. Fimbrial. 1 hit.
PF09160. FimH_man-bind. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08191-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:300
Mass (Da):31,473
Last modified:February 1, 1995 - v2
Checksum:i939204A51658747D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791L → R (PubMed:7905476).Curated
Sequence conflicti197 – 1971P → R in CAA29156 (PubMed:2890081).Curated
Sequence conflicti222 – 2221T → H (PubMed:2890081).Curated
Sequence conflicti222 – 2221T → H (PubMed:7905476).Curated

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.
PIRiS56545.
RefSeqiNP_418740.1. NC_000913.3.
WP_000832247.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77276; AAC77276; b4320.
BAE78313; BAE78313; BAE78313.
GeneIDi948847.
KEGGiecj:JW4283.
eco:b4320.
PATRICi32124236. VBIEscCol129921_4461.

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.
PIRiS56545.
RefSeqiNP_418740.1. NC_000913.3.
WP_000832247.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KIUX-ray3.00B/D/F/H/J/L/N/P22-300[»]
1KLFX-ray2.79B/D/F/H/J/L/N/P22-300[»]
1QUNX-ray2.80B/D/F/H/J/L/N/P22-300[»]
1TR7X-ray2.10A/B22-179[»]
1UWFX-ray1.69A22-179[»]
1ZE3X-ray1.84H179-300[»]
2VCOX-ray2.10A/B22-179[»]
3RFZX-ray2.80A/D22-300[»]
3ZL1X-ray1.55A/B22-179[»]
3ZL2X-ray1.25A22-179[»]
4ATTX-ray1.25A22-179[»]
4AUJX-ray1.53A22-179[»]
4AUUX-ray1.60A/B22-179[»]
4AUYX-ray2.10A/B22-179[»]
4AV0X-ray2.10A/B22-179[»]
4AV4X-ray1.90A22-179[»]
4AV5X-ray1.40A/B/C/D22-179[»]
4AVHX-ray2.10A/B22-179[»]
4AVIX-ray2.40A/B22-179[»]
4AVJX-ray2.10A/B22-179[»]
4AVKX-ray2.40A/B22-179[»]
4CSSX-ray1.07A22-180[»]
4CSTX-ray1.10A22-180[»]
4J3OX-ray3.80H22-300[»]
4LOVX-ray1.50A22-179[»]
4X50X-ray2.00A/B22-180[»]
4X5PX-ray1.00A22-180[»]
4X5QX-ray1.12A22-180[»]
4X5RX-ray1.65A/B/C22-180[»]
4XO8X-ray1.70A/B22-179[»]
4XO9X-ray1.14A22-300[»]
4XOAX-ray2.54A/C/E/G22-300[»]
4XOBX-ray3.00A/C/E/G22-300[»]
4XODX-ray1.14A22-300[»]
5AB1X-ray1.96A/B1-300[»]
5ABZX-ray2.40A/B22-179[»]
5F2FX-ray1.67A22-179[»]
ProteinModelPortaliP08191.
SMRiP08191. Positions 22-300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262737. 8 interactions.
DIPiDIP-9616N.
IntActiP08191. 2 interactions.
STRINGi511145.b4320.

Chemistry

BindingDBiP08191.
ChEMBLiCHEMBL4837.

Proteomic databases

PaxDbiP08191.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77276; AAC77276; b4320.
BAE78313; BAE78313; BAE78313.
GeneIDi948847.
KEGGiecj:JW4283.
eco:b4320.
PATRICi32124236. VBIEscCol129921_4461.

Organism-specific databases

EchoBASEiEB0311.
EcoGeneiEG10315. fimH.

Phylogenomic databases

eggNOGiENOG410643X. Bacteria.
ENOG410Y3E1. LUCA.
HOGENOMiHOG000120719.
KOiK07350.
OMAiDYPGSMA.

Enzyme and pathway databases

BioCyciEcoCyc:EG10315-MONOMER.
ECOL316407:JW4283-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP08191.
PROiP08191.

Family and domain databases

CDDicd10466. FimH_man-bind. 1 hit.
Gene3Di2.60.40.1090. 2 hits.
InterProiIPR008966. Adhesion_dom.
IPR000259. Adhesion_dom_fimbrial.
IPR015243. FimH_man-bd.
[Graphical view]
PfamiPF00419. Fimbrial. 1 hit.
PF09160. FimH_man-bind. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiFIMH_ECOLI
AccessioniPrimary (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: September 7, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.