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UniProtKB - P21514 (PDEL_ECOLI)

Entry version 147 (13 Nov 2019)
Sequence version 2 (01 Nov 1997)
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Protein

Cyclic di-GMP phosphodiesterase PdeL

Gene

pdeL

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

Acts both as an enzyme and as a c-di-GMP sensor to couple transcriptional activity to the c-di-GMP status of the cell (PubMed:26553851). Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG (PubMed:15995192, PubMed:24451384, PubMed:26553851). Also acts as a transcription factor to control its own expression (PubMed:26553851).3 Publications

Miscellaneous

An overexpressed EAL domain (residues 77-362) has similar KM, Vmax, pH and metal dependence and subunit composition as the full-length protein.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+2 Publications, Mn2+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Strongly inhibited by Ca2+.2 Publications

<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=25 µM for c-di-GMP1 Publication

    pH dependencei

    Optimum pH is 9.35.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei127SubstrateCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi141Magnesium or manganeseCombined sources1 Publication1
    Metal bindingi200Magnesium or manganeseCombined sources1 Publication1
    Binding sitei200SubstrateCombined sources1 Publication1
    Metal bindingi232Magnesium or manganeseCombined sources1 Publication1
    Metal bindingi262Magnesium or manganeseCombined sources1 Publication1
    Binding sitei262SubstrateCombined sources1 Publication1
    Binding sitei286SubstrateCombined sources1 Publication1
    Binding sitei341SubstrateCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi42 – 61H-T-H motifPROSITE-ProRule annotationAdd BLAST20

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    • positive regulation of transcription, DNA-templated Source: EcoCyc
    Complete GO annotation on QuickGO ...

    <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

    Molecular functionDNA-binding, Hydrolase
    Biological processTranscription, Transcription regulation
    Ligandc-di-GMP, Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:EG11236-MONOMER
    ECOL316407:JW0307-MONOMER
    MetaCyc:EG11236-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P21514

    <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:
    Cyclic di-GMP phosphodiesterase PdeLCurated (EC:3.1.4.523 Publications)
    <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:pdeL1 Publication
    Synonyms:yahA
    Ordered Locus Names:b0315, JW0307
    <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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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 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>Mutagenesisi60K → A: Does not bind to the PdeL box. 1 Publication1
    Mutagenesisi206F → S: Increases catalytic activity. 1 Publication1
    Mutagenesisi249F → L: Increases catalytic activity. 1 Publication1
    Mutagenesisi263D → N: Loss of activity. 1 Publication1
    Mutagenesisi298S → W: Slow monomer-dimer exchange. Equilibrium largely on the monomeric side, in particular in the presence of substrate. Strong decrease in activity. 1 Publication1
    Mutagenesisi299G → S: Increases catalytic activity. 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_00001685731 – 362Cyclic di-GMP phosphodiesterase PdeLAdd BLAST362

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P21514

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

    More...    PaxDbi    		P21514

    PRoteomics IDEntifications database

    More...    PRIDEi    		P21514

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Autoregulated. Directly regulates its own expression in a c-di-GMP-dependent manner.1 Publication

    <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

    Is in a fast thermodynamic monomer-homodimer equilibrium. Dimerization is required for PDE activity. Dimerization affinity is increased about 100-fold upon substrate binding.

    1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4262803, 8 interactors

    Protein interaction database and analysis system

    More...    IntActi    		P21514, 3 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0315

    <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

    1362
    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    		P21514

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini18 – 83HTH luxR-typePROSITE-ProRule annotationAdd BLAST66
    Domaini106 – 360EALPROSITE-ProRule annotationAdd BLAST255

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni144 – 145Substrate bindingCombined sources1 Publication2
    Regioni319 – 322Substrate bindingCombined sources1 Publication4

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105BZU Bacteria
    COG2200 LUCA
    COG2771 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000117345

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P21514

    KEGG Orthology (KO)

    More...    KOi    		K13244

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P21514

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd01948 EAL, 1 hit
    cd06170 LuxR_C_like, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		1.10.10.10, 1 hit
    3.20.20.450, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR001633 EAL_dom
    IPR035919 EAL_sf
    IPR016032 Sig_transdc_resp-reg_C-effctor
    IPR000792 Tscrpt_reg_LuxR_C
    IPR036388 WH-like_DNA-bd_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00563 EAL, 1 hit
    PF00196 GerE, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00052 EAL, 1 hit
    SM00421 HTH_LUXR, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF141868 SSF141868, 1 hit
    SSF46894 SSF46894, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS50883 EAL, 1 hit
    PS50043 HTH_LUXR_2, 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>. 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.

    P21514-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNSCDFRVFL QEFGTTVHLS LPGSVSEKER LLLKLLMQGM SVTEISQYRN 
            60         70         80         90        100
    RSAKTISHQK KQLFEKLGIQ SDITFWRDIF FQYNPEIISA TGSNSHRYIN 
           110        120        130        140        150
    DNHYHHIVTP EAISLALENH EFKPWIQPVF CAQTGVLTGC EVLVRWEHPQ 
           160        170        180        190        200
    TGIIPPDQFI PLAESSGLIV IMTRQLMKQT ADILMPVKHL LPDNFHIGIN 
           210        220        230        240        250
    VSAGCFLAAG FEKECLNLVN KLGNDKIKLV LELTERNPIP VTPEARAIFD 
           260        270        280        290        300
    SLHQHNITFA LDDFGTGYAT YRYLQAFPVD FIKIDKSFVQ MASVDEISGH 
           310        320        330        340        350
    IVDNIVELAR KPGLSIVAEG VETQEQADLM IGKGVHFLQG YLYSPPVPGN 
           360 
    KFISEWVMKA GG
    Length:362
    Mass (Da):40,725
    Last modified:November 1, 1997 - 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:i4BCA091840F27A0D
    GO

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAB18041 differs from that shown. Reason: Erroneous initiation.Curated

    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
    		U73857 Genomic DNA Translation: AAB18041.1 Different initiation.
    U00096 Genomic DNA Translation: AAC73418.1
    AP009048 Genomic DNA Translation: BAE76098.1
    X52905 Genomic DNA Translation: CAA37089.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		C64758

    NCBI Reference Sequences

    More...    RefSeqi    		NP_414849.1, NC_000913.3
    WP_001301264.1, NZ_SSZK01000075.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73418; AAC73418; b0315
    BAE76098; BAE76098; BAE76098

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		947459

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0307
    eco:b0315

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.1962

    <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
    		U73857 Genomic DNA Translation: AAB18041.1 Different initiation.
    U00096 Genomic DNA Translation: AAC73418.1
    AP009048 Genomic DNA Translation: BAE76098.1
    X52905 Genomic DNA Translation: CAA37089.1
    PIRiC64758
    RefSeqiNP_414849.1, NC_000913.3
    WP_001301264.1, NZ_SSZK01000075.1

    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
    4KIEX-ray1.70A96-362[»]
    4LJ3X-ray1.70A/B101-362[»]
    4LYKX-ray2.40A/B/C/D101-362[»]
    SMRiP21514
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4262803, 8 interactors
    IntActiP21514, 3 interactors
    STRINGi511145.b0315

    Proteomic databases

    jPOSTiP21514
    PaxDbiP21514
    PRIDEiP21514

    Genome annotation databases

    EnsemblBacteriaiAAC73418; AAC73418; b0315
    BAE76098; BAE76098; BAE76098
    GeneIDi947459
    KEGGiecj:JW0307
    eco:b0315
    PATRICifig|1411691.4.peg.1962

    Organism-specific databases

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

    More...    EchoBASEi    		EB1218

    Phylogenomic databases

    eggNOGiENOG4105BZU Bacteria
    COG2200 LUCA
    COG2771 LUCA
    HOGENOMiHOG000117345
    InParanoidiP21514
    KOiK13244
    PhylomeDBiP21514

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11236-MONOMER
    ECOL316407:JW0307-MONOMER
    MetaCyc:EG11236-MONOMER
    SABIO-RKiP21514

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P21514

    Family and domain databases

    CDDicd01948 EAL, 1 hit
    cd06170 LuxR_C_like, 1 hit
    Gene3Di1.10.10.10, 1 hit
    3.20.20.450, 1 hit
    InterProiView protein in InterPro
    IPR001633 EAL_dom
    IPR035919 EAL_sf
    IPR016032 Sig_transdc_resp-reg_C-effctor
    IPR000792 Tscrpt_reg_LuxR_C
    IPR036388 WH-like_DNA-bd_sf
    PfamiView protein in Pfam
    PF00563 EAL, 1 hit
    PF00196 GerE, 1 hit
    SMARTiView protein in SMART
    SM00052 EAL, 1 hit
    SM00421 HTH_LUXR, 1 hit
    SUPFAMiSSF141868 SSF141868, 1 hit
    SSF46894 SSF46894, 1 hit
    PROSITEiView protein in PROSITE
    PS50883 EAL, 1 hit
    PS50043 HTH_LUXR_2, 1 hit

    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 nameiPDEL_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: P21514
    Secondary accession number(s): P75689, Q2MCA8
    <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: May 1, 1991
    Last sequence update: November 1, 1997
    Last modified: November 13, 2019
    This is version 147 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, 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
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