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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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 databases

ChEMBLiCHEMBL3124740.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000000921122 – 300Protein FimHAdd BLAST279

Proteomic databases

PaxDbiP08191.
PRIDEiP08191.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP08191.

Structurei

Secondary structure

1300
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 26Combined sources4
Beta strandi37 – 43Combined sources7
Beta strandi48 – 50Combined sources3
Beta strandi55 – 58Combined sources4
Helixi59 – 61Combined sources3
Beta strandi63 – 66Combined sources4
Turni70 – 72Combined sources3
Beta strandi75 – 84Combined sources10
Helixi86 – 91Combined sources6
Beta strandi92 – 98Combined sources7
Beta strandi101 – 106Combined sources6
Beta strandi114 – 116Combined sources3
Beta strandi118 – 120Combined sources3
Beta strandi126 – 132Combined sources7
Beta strandi134 – 136Combined sources3
Beta strandi138 – 141Combined sources4
Beta strandi146 – 159Combined sources14
Beta strandi163 – 173Combined sources11
Beta strandi175 – 177Combined sources3
Beta strandi180 – 185Combined sources6
Beta strandi187 – 192Combined sources6
Beta strandi195 – 197Combined sources3
Beta strandi200 – 202Combined sources3
Beta strandi205 – 210Combined sources6
Beta strandi212 – 220Combined sources9
Beta strandi222 – 224Combined sources3
Beta strandi235 – 238Combined sources4
Beta strandi240 – 248Combined sources9
Beta strandi259 – 264Combined sources6
Beta strandi273 – 279Combined sources7
Beta strandi281 – 283Combined sources3
Beta strandi286 – 299Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5CGBX-ray1.60A/B22-179[»]
5F2FX-ray1.67A22-179[»]
ProteinModelPortaliP08191.
SMRiP08191.
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)DescriptionActionsGraphical viewLength
Sequence conflicti79L → R (PubMed:7905476).Curated1
Sequence conflicti197P → R in CAA29156 (PubMed:2890081).Curated1
Sequence conflicti222T → H (PubMed:2890081).Curated1
Sequence conflicti222T → H (PubMed:7905476).Curated1

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
PDB 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[»]
5CGBX-ray1.60A/B22-179[»]
5F2FX-ray1.67A22-179[»]
ProteinModelPortaliP08191.
SMRiP08191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP08191.
ChEMBLiCHEMBL3124740.

Proteomic databases

PaxDbiP08191.
PRIDEiP08191.

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: November 30, 2016
This is version 145 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.