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

Multidrug transporter EmrE

Gene

emrE

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

Annotation score:5 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

Multidrug transporter that expels positively charged hydrophobic drugs across the inner membrane of E.coli., thereby conferring resistance to a wide range of toxic compounds. The drug efflux is coupled to an influx of protons. Is involved in the resistance of E.coli cells to methyl viologen, ethidium bromide and acriflavine. Is also able to transport tetraphenylphosphonium (TPP+) and benzalkonium.4 Publications

Miscellaneous

Encoded by the cryptic lambdoid prophage DLP12.

Caution

EM structures show an asymmetric dimer with the monomers in an antiparallel orientation, in contradiction with biochemical data and cross-linking studies, which demonstrated a parallel arrangement. Until now, EmrE with a parallel orientation is the only one to be shown to be fully functional.Curated

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=247 µM for methyl viologen1 Publication
  1. Vmax=1572 nmol/min/mg enzyme with methyl viologen as substrate1 Publication

pH dependencei

Optimum pH is 8-8.5. Transport activity occurs from pH 7.5 to 9.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei4Required for proper coupling between the substrate transport and the proton gradient1
Sitei14Essential for translocation and for substrate and proton binding1
Sitei40Involved in substrate binding1
Sitei60Involved in substrate binding1
Sitei63Involved in substrate binding1

<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

  • amino-acid betaine transmembrane transporter activity Source: EcoCyc
  • antiporter activity Source: EcoliWiki
  • choline transmembrane transporter activity Source: EcoCyc
  • drug:proton antiporter activity Source: EcoCyc
  • identical protein binding Source: IntAct
  • transmembrane transporter activity Source: CACAO

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • choline transport Source: EcoCyc
  • glycine betaine transport Source: EcoCyc
  • response to drug Source: EcoliWiki
  • response to osmotic stress Source: EcoCyc
  • transmembrane transport Source: GO_Central
  • xenobiotic metabolic process Source: EcoliWiki

<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>Keywordsi

Biological processAntiport, Transport

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EMRE-MONOMER
MetaCyc:EMRE-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P23895

Protein family/group databases

Transport Classification Database

More...
TCDBi
2.A.7.1.3 the drug/metabolite transporter (dmt) superfamily

<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:
Multidrug transporter EmrE
Alternative name(s):
Efflux-multidrug resistance protein EmrE
Ethidium resistance protein
Methyl viologen resistance protein C
<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:emrE
Synonyms:eb, mvrC
Ordered Locus Names:b0543, JW0531
<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

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10629 emrE

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 3Cytoplasmic3
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei4 – 21Helical; Name=1Add BLAST18
Topological domaini22 – 33PeriplasmicAdd BLAST12
Transmembranei34 – 52Helical; Name=2Add BLAST19
Topological domaini53 – 57Cytoplasmic5
Transmembranei58 – 81Helical; Name=3Add BLAST24
Topological domaini82 – 84Periplasmic3
Transmembranei85 – 105Helical; Name=4Add BLAST21
Topological domaini106 – 110Cytoplasmic5

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi4Y → C: Still binds substrate. No transport activity in the presence of a proton gradient, but still transports substrate in the absence of a proton gradient. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi4Y → F or W: No effect on resistance to toxicants. 1 Publication1
Mutagenesisi6Y → C, F or L: No effect on resistance to toxicants. 1 Publication1
Mutagenesisi7L → C: No substrate binding. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi10A → C: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi11I → C: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi14E → C: No substrate binding. No transport activity. Resistance to toxicants is abolished. 2 Publications1
Mutagenesisi14E → D: Still binds substrate. No transport activity in the presence of a proton gradient, but still transports substrate in the absence of a proton gradient. Resistance to toxicants is abolished. 2 Publications1
Mutagenesisi17G → C: No substrate binding. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi18T → C: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi40Y → C, F, L, M, S, T or V: Modifies substrate specificity. 1 Publication1
Mutagenesisi53Y → C: No effect on resistance to toxicants. 1 Publication1
Mutagenesisi60Y → C or F: Still binds substrate, with lower affinity. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi63W → C or Y: No transport activity. Resistance to toxicants is abolished. 1 Publication1
Mutagenesisi63W → F: Still binds substrate, with two-fold reduction in substrate affinity. Resistance to toxicants is abolished. 1 Publication1

<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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001080741 – 110Multidrug transporter EmrEAdd BLAST110

Proteomic databases

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

More...
PaxDbi
P23895

PRoteomics IDEntifications database

More...
PRIDEi
P23895

<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">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; parallel. May also form dimer of homodimers. Binds substrate at the dimerization interface.5 Publications

<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

WithEntry#Exp.IntActNotes
itself2EBI-8789431,EBI-8789431

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259366, 101 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2121 EmrE complex

Database of interacting proteins

More...
DIPi
DIP-9505N

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0499

<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

1110
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
2I68electron microscopy-A/B1-110[»]
3B5DX-ray3.80A/B1-110[»]
3B61X-ray4.50A/B/C/D/E/F/G/H1-110[»]
3B62X-ray4.40A/B/C/D1-110[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P23895

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

More...
SMRi
P23895

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P23895

<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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410814C Bacteria
COG2076 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000268006

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P23895

KEGG Orthology (KO)

More...
KOi
K03297

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P23895

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000390 Small_multidrug_res

The PANTHER Classification System

More...
PANTHERi
PTHR30561 PTHR30561, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00893 Multi_Drug_Res, 1 hit

<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>.<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.

P23895-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNPYIYLGGA ILAEVIGTTL MKFSEGFTRL WPSVGTIICY CASFWLLAQT
60 70 80 90 100
LAYIPTGIAY AIWSGVGIVL ISLLSWGFFG QRLDLPAIIG MMLICAGVLI
110
INLLSRSTPH
Length:110
Mass (Da):11,958
Last modified:November 1, 1991 - v1
<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:i775153FC47D6AE3D
GO

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
Z11877 Genomic DNA Translation: CAA77936.1
M62732 Genomic DNA Translation: AAA24190.1
U82598 Genomic DNA Translation: AAB40740.1
U00096 Genomic DNA Translation: AAC73644.1
AP009048 Genomic DNA Translation: BAE76318.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JN0329

NCBI Reference Sequences

More...
RefSeqi
NP_415075.1, NC_000913.3
WP_001070439.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73644; AAC73644; b0543
BAE76318; BAE76318; BAE76318

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948442

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0531
eco:b0543

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1735

<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
Z11877 Genomic DNA Translation: CAA77936.1
M62732 Genomic DNA Translation: AAA24190.1
U82598 Genomic DNA Translation: AAB40740.1
U00096 Genomic DNA Translation: AAC73644.1
AP009048 Genomic DNA Translation: BAE76318.1
PIRiJN0329
RefSeqiNP_415075.1, NC_000913.3
WP_001070439.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I68electron microscopy-A/B1-110[»]
3B5DX-ray3.80A/B1-110[»]
3B61X-ray4.50A/B/C/D/E/F/G/H1-110[»]
3B62X-ray4.40A/B/C/D1-110[»]
ProteinModelPortaliP23895
SMRiP23895
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259366, 101 interactors
ComplexPortaliCPX-2121 EmrE complex
DIPiDIP-9505N
STRINGi316385.ECDH10B_0499

Protein family/group databases

TCDBi2.A.7.1.3 the drug/metabolite transporter (dmt) superfamily

Proteomic databases

PaxDbiP23895
PRIDEiP23895

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
948442
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73644; AAC73644; b0543
BAE76318; BAE76318; BAE76318
GeneIDi948442
KEGGiecj:JW0531
eco:b0543
PATRICifig|1411691.4.peg.1735

Organism-specific databases

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

More...
EchoBASEi
EB0623
EcoGeneiEG10629 emrE

Phylogenomic databases

eggNOGiENOG410814C Bacteria
COG2076 LUCA
HOGENOMiHOG000268006
InParanoidiP23895
KOiK03297
PhylomeDBiP23895

Enzyme and pathway databases

BioCyciEcoCyc:EMRE-MONOMER
MetaCyc:EMRE-MONOMER
SABIO-RKiP23895

Miscellaneous databases

EvolutionaryTraceiP23895

Protein Ontology

More...
PROi
PR:P23895

Family and domain databases

InterProiView protein in InterPro
IPR000390 Small_multidrug_res
PANTHERiPTHR30561 PTHR30561, 1 hit
PfamiView protein in Pfam
PF00893 Multi_Drug_Res, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiEMRE_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: P23895
Secondary accession number(s): Q2MBN8
<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: November 1, 1991
Last sequence update: November 1, 1991
Last modified: January 16, 2019
This is version 150 of the entry and version 1 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again