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Entry version 167 (13 Nov 2019)
Sequence version 2 (01 Feb 1995)
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Protein

Type 1 fimbrin D-mannose specific adhesin

Gene

fimH

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

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • mannose binding Source: EcoCyc

GO - Biological processi

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10315-MONOMER
ECOL316407:JW4283-MONOMER

Protein family/group databases

UniLectin database of carbohydrate-binding proteins

More...
UniLectini
P08191

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Type 1 fimbrin D-mannose specific adhesin
Alternative name(s):
Protein FimH
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:fimH
Ordered Locus Names:b4320, JW4283
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti

Fimbrium

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3124740
CHEMBL4837

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 211 PublicationAdd BLAST21
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000921122 – 300Type 1 fimbrin D-mannose specific adhesinAdd BLAST279

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P08191

PRoteomics IDEntifications database

More...
PRIDEi
P08191

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262737, 8 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2855 Fimbrial Tip Complex FimFGH

Database of interacting proteins

More...
DIPi
DIP-9616N

Protein interaction database and analysis system

More...
IntActi
P08191, 3 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b4320

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P08191

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1300
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P08191

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P08191

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the fimbrial protein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410643X Bacteria
ENOG410Y3E1 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000120719

KEGG Orthology (KO)

More...
KOi
K07350

Family and domain databases

Conserved Domains Database

More...
CDDi
cd10466 FimH_man-bind, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1090, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000259 Adhesion_dom_fimbrial
IPR036937 Adhesion_dom_fimbrial_sf
IPR008966 Adhesion_dom_sf
IPR015243 FimH_man-bd

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00419 Fimbrial, 1 hit
PF09160 FimH_man-bind, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49401 SSF49401, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i939204A51658747D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
S56545

NCBI Reference Sequences

More...
RefSeqi
NP_418740.1, NC_000913.3
WP_000832247.1, NZ_SSUV01000012.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC77276; AAC77276; b4320
BAE78313; BAE78313; BAE78313

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948847

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW4283
eco:b4320

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2372

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_SSUV01000012.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
5FS5X-ray1.42A22-179[»]
5FWRX-ray2.13A/B/C/D/E/F/G/H22-179[»]
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[»]
6E14electron microscopy4.00H1-300[»]
6E15electron microscopy6.20H1-300[»]
6G2RX-ray2.10A/B22-179[»]
6G2SX-ray2.20A/B/C/D/E/F/G/H/I22-179[»]
6GTXX-ray2.50A/B/C/D22-179[»]
6GTYX-ray1.90A/B/C/D/E22-179[»]
SMRiP08191
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4262737, 8 interactors
ComplexPortaliCPX-2855 Fimbrial Tip Complex FimFGH
DIPiDIP-9616N
IntActiP08191, 3 interactors
STRINGi511145.b4320

Chemistry databases

BindingDBiP08191
ChEMBLiCHEMBL3124740
CHEMBL4837

Protein family/group databases

UniLectiniP08191

Proteomic databases

PaxDbiP08191
PRIDEiP08191

Genome annotation databases

EnsemblBacteriaiAAC77276; AAC77276; b4320
BAE78313; BAE78313; BAE78313
GeneIDi948847
KEGGiecj:JW4283
eco:b4320
PATRICifig|1411691.4.peg.2372

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0311

Phylogenomic databases

eggNOGiENOG410643X Bacteria
ENOG410Y3E1 LUCA
HOGENOMiHOG000120719
KOiK07350

Enzyme and pathway databases

BioCyciEcoCyc:EG10315-MONOMER
ECOL316407:JW4283-MONOMER

Miscellaneous databases

EvolutionaryTraceiP08191

Protein Ontology

More...
PROi
PR:P08191

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFIMH_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08191
Secondary accession number(s): Q2M5Z3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1995
Last modified: November 13, 2019
This is version 167 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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