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Protein

Type 1 fimbrin D-mannose specific adhesin

Gene

fimH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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.1 Publication

GO - Molecular functioni

  • mannose binding Source: EcoCyc

GO - Biological processi

  • cell adhesion Source: EcoCyc

Enzyme and pathway databases

BioCyciEcoCyc:EG10315-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Type 1 fimbrin D-mannose specific adhesin
Alternative name(s):
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

  • Fimbrium 1 Publication

GO - Cellular componenti

  • host cell membrane Source: UniProtKB
  • pilus Source: EcoCyc

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 – 300Type 1 fimbrin D-mannose specific adhesinAdd BLAST279

Proteomic databases

PaxDbiP08191
PRIDEiP08191

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi4262737, 8 interactors
DIPiDIP-9616N
IntActiP08191, 3 interactors
STRINGi316407.85677063

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[»]
5F3FX-ray1.76A22-179[»]
5FX3X-ray1.90A22-179[»]
5JCQX-ray1.60A/B22-179[»]
5JCRX-ray1.70A/B22-179[»]
5L4TX-ray1.90A/B22-179[»]
5L4UX-ray2.10A/B22-179[»]
5L4VX-ray2.99A/B/C22-179[»]
5L4WX-ray1.90A/B/C22-179[»]
5L4XX-ray1.90A/B22-179[»]
5L4YX-ray1.90A/B22-179[»]
5MCAX-ray1.60A22-180[»]
5MTSX-ray2.60A/B1-300[»]
5MUCX-ray2.60A/B22-179[»]
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
InterProiView protein in InterPro
IPR000259 Adhesion_dom_fimbrial
IPR036937 Adhesion_dom_fimbrial_sf
IPR008966 Adhesion_dom_sf
IPR015243 FimH_man-bd
PfamiView protein in Pfam
PF00419 Fimbrial, 1 hit
PF09160 FimH_man-bind, 1 hit
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 no nucleotide entry (PubMed:7905476).Curated1
Sequence conflicti197P → R in CAA29156 (PubMed:2890081).Curated1
Sequence conflicti222T → H in CAA29156 (PubMed:2890081).Curated1
Sequence conflicti222T → H no nucleotide entry (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
PATRICifig|1411691.4.peg.2372

Similar proteinsi

Entry informationi

Entry nameiFIMH_ECOLI
AccessioniPrimary (citable) accession number: P08191
Secondary accession number(s): Q2M5Z3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1995
Last modified: March 28, 2018
This is version 155 of the entry and version 2 of the sequence. See 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

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