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Entry version 125 (07 Oct 2020)
Sequence version 1 (10 May 2005)
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Protein

GTPase Der

Gene

der

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

GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defective and unable to assemble into 70S ribosomes. GTPase activity is stimulated by YihI. Overexpression rescues an rrmJ deletion, stabilizing the 70S ribosome. Der and RrmJ are likely to share a mechanism to stabilize 50S ribosomal subunits at a very late stage of 50S subunit maturation possibly by interacting with 23S rRNA or 23S rRNA/r-protein complex.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

Vmax increases 35% in the presence of full-length YihI and 90% in the presence of YihI missing the first 45 residues.
  1. KM=125 µM for GTP (to 143 µM) in the absence of YihI2 Publications
  2. KM=59.2 µM for GTP in the presence of full-length YihI2 Publications
  3. KM=50.1 µM for GTP in the presence of N-terminally truncated YihI2 Publications

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi9 – 16GTP 1Sequence analysis8
    Nucleotide bindingi56 – 60GTP 1Sequence analysis5
    Nucleotide bindingi118 – 121GTP 1Sequence analysis4
    Nucleotide bindingi209 – 216GTP 2Sequence analysis8
    Nucleotide bindingi256 – 260GTP 2Sequence analysis5
    Nucleotide bindingi321 – 324GTP 2Sequence analysis4

    <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

    GO - Biological processi

    • ribosomal large subunit assembly Source: EcoCyc

    <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 processRibosome biogenesis
    LigandGTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:G7319-MONOMER
    MetaCyc:G7319-MONOMER

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    GTPase Der
    Alternative name(s):
    Double era-like domain protein
    GTP-binding protein EngA
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:der
    Synonyms:engA, yfgK
    Ordered Locus Names:b2511, JW5403
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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>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

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Lethality. In a depletion experiment cells grow normally for 4 hours, at which time there is no detectable protein left. After 4 hours cell growth decreases rapidly, the amount of 50S ribosomal subunit decreases, rRNA precursors accumulate. A 40S ribosomal subunit is detected which is missing proteins L9 and L18 and has slightly reduced amounts of L2 and L6 compared to wild-type ribosomes.3 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi15K → A: Complements a disruption mutant, KM for GTP 695 uM. 1 Publication1
    Mutagenesisi16S → A: Does not complement a disruption mutant, KM for GTP 4.9 mM. Decreased GTPase activity, no stimulation by YihI. 2 Publications1
    Mutagenesisi118N → D: Complements a disruption mutant at 42 degrees Celsius, very poor complementation at 30 degrees Celsius. Reduces affinity for the 50S ribosomal subunit at 30 degrees Celsius. RelA suppresses this point mutation at 30 degrees Celsius. 1 Publication1
    Mutagenesisi118N → D: Does not complement a disruption mutant at 42 degrees Celsius, diminished association with 50S ribosomal subunits; when associated with D-321. 1 Publication1
    Mutagenesisi215K → A: Does not complement a disruption mutant, KM for GTP 6.7 mM. 1 Publication1
    Mutagenesisi216S → A: Does not complement a disruption mutant, considerably decreased GTPase activity, KM for GTP 4.8 mM, no stimulation by YihI. 2 Publications1
    Mutagenesisi321N → D: Complements a disruption mutant at 42 degrees Celsius, no complementation at 30 degrees Celsius. Greatly reduces affinity for the 50S ribosomal subunit at 30 degrees Celsius. RelA suppresses this point mutation at 30 degrees Celsius. 1 Publication1
    Mutagenesisi414G → R: Does not complement rrmJ deletion, complements der disruption at 42 degrees Celsius. 1 Publication1
    Mutagenesisi424G → D: Does not complement rrmJ deletion, nor the der disruption at 42 degrees Celsius. 1 Publication1
    Mutagenesisi469N → K: Does not complement rrmJ deletion, complements der disruption at 42 degrees Celsius. 1 Publication1
    Mutagenesisi472T → A: Does not complement rrmJ deletion, complements der disruption at 42 degrees Celsius. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001789911 – 490GTPase DerAdd BLAST490

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0A6P5

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

    More...
    PaxDbi
    P0A6P5

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A6P5

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Associates with the 50S ribosomal subunit in the presence of GMPPNP, a non-hydrolysable GTP analog, and thus probably also in the presence of GTP, but not in the presence of GDP or in the absence of nucleotide.

    Interacts with YihI via the last 490 residues.

    3 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4263153, 69 interactors
    851322, 1 interactor

    Database of interacting proteins

    More...
    DIPi
    DIP-48272N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A6P5, 7 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2511

    <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

    3D structure databases

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

    More...
    SMRi
    P0A6P5

    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%5Fand%5Fdomains%5Fsection">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>Domaini3 – 166EngA-type G 1Add BLAST164
    Domaini203 – 376EngA-type G 2Add BLAST174
    Domaini377 – 461KH-likeAdd BLAST85

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The 2 G (guanine nucleotide-binding) domains are essential for activity and function cooperatively. The KH-like domain is required for ribosome recognition.1 Publication

    <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

    Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG1160, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_016077_6_2_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A6P5

    KEGG Orthology (KO)

    More...
    KOi
    K03977

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A6P5

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.300.20, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00195, GTPase_Der, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR031166, G_ENGA
    IPR016484, GTP-bd_EngA
    IPR006073, GTP_binding_domain
    IPR032859, KH_dom-like
    IPR015946, KH_dom-like_a/b
    IPR027417, P-loop_NTPase
    IPR005225, Small_GTP-bd_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF14714, KH_dom-like, 1 hit
    PF01926, MMR_HSR1, 2 hits

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF006485, GTP-binding_EngA, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00326, GTP1OBG

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52540, SSF52540, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR03594, GTPase_EngA, 1 hit
    TIGR00231, small_GTP, 2 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51712, G_ENGA, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P0A6P5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MVPVVALVGR PNVGKSTLFN RLTRTRDALV ADFPGLTRDR KYGRAEIEGR
    60 70 80 90 100
    EFICIDTGGI DGTEDGVETR MAEQSLLAIE EADVVLFMVD ARAGLMPADE
    110 120 130 140 150
    AIAKHLRSRE KPTFLVANKT DGLDPDQAVV DFYSLGLGEI YPIAASHGRG
    160 170 180 190 200
    VLSLLEHVLL PWMEDLAPQE EVDEDAEYWA QFEAEENGEE EEEDDFDPQS
    210 220 230 240 250
    LPIKLAIVGR PNVGKSTLTN RILGEERVVV YDMPGTTRDS IYIPMERDGR
    260 270 280 290 300
    EYVLIDTAGV RKRGKITDAV EKFSVIKTLQ AIEDANVVML VIDAREGISD
    310 320 330 340 350
    QDLSLLGFIL NSGRSLVIVV NKWDGLSQEV KEQVKETLDF RLGFIDFARV
    360 370 380 390 400
    HFISALHGSG VGNLFESVRE AYDSSTRRVG TSMLTRIMTM AVEDHQPPLV
    410 420 430 440 450
    RGRRVKLKYA HAGGYNPPIV VIHGNQVKDL PDSYKRYLMN YFRKSLDVMG
    460 470 480 490
    SPIRIQFKEG ENPYANKRNT LTPTQMRKRK RLMKHIKKNK
    Length:490
    Mass (Da):55,036
    Last modified:May 10, 2005 - 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:i0321511F5A5A7E3D
    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
    U00096 Genomic DNA Translation: AAC75564.2
    AP009048 Genomic DNA Translation: BAA16397.2

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    F65027

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417006.2, NC_000913.3
    WP_000249410.1, NZ_STEB01000011.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75564; AAC75564; b2511
    BAA16397; BAA16397; BAA16397

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946983

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW5403
    eco:b2511

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.4225

    <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
    U00096 Genomic DNA Translation: AAC75564.2
    AP009048 Genomic DNA Translation: BAA16397.2
    PIRiF65027
    RefSeqiNP_417006.2, NC_000913.3
    WP_000249410.1, NZ_STEB01000011.1

    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
    3J8Gelectron microscopy5.00X1-490[»]
    SMRiP0A6P5
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4263153, 69 interactors
    851322, 1 interactor
    DIPiDIP-48272N
    IntActiP0A6P5, 7 interactors
    STRINGi511145.b2511

    Proteomic databases

    jPOSTiP0A6P5
    PaxDbiP0A6P5
    PRIDEiP0A6P5

    Genome annotation databases

    EnsemblBacteriaiAAC75564; AAC75564; b2511
    BAA16397; BAA16397; BAA16397
    GeneIDi946983
    KEGGiecj:JW5403
    eco:b2511
    PATRICifig|1411691.4.peg.4225

    Organism-specific databases

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

    More...
    EchoBASEi
    EB3959

    Phylogenomic databases

    eggNOGiCOG1160, Bacteria
    HOGENOMiCLU_016077_6_2_6
    InParanoidiP0A6P5
    KOiK03977
    PhylomeDBiP0A6P5

    Enzyme and pathway databases

    BioCyciEcoCyc:G7319-MONOMER
    MetaCyc:G7319-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P0A6P5

    Family and domain databases

    Gene3Di3.30.300.20, 1 hit
    HAMAPiMF_00195, GTPase_Der, 1 hit
    InterProiView protein in InterPro
    IPR031166, G_ENGA
    IPR016484, GTP-bd_EngA
    IPR006073, GTP_binding_domain
    IPR032859, KH_dom-like
    IPR015946, KH_dom-like_a/b
    IPR027417, P-loop_NTPase
    IPR005225, Small_GTP-bd_dom
    PfamiView protein in Pfam
    PF14714, KH_dom-like, 1 hit
    PF01926, MMR_HSR1, 2 hits
    PIRSFiPIRSF006485, GTP-binding_EngA, 1 hit
    PRINTSiPR00326, GTP1OBG
    SUPFAMiSSF52540, SSF52540, 2 hits
    TIGRFAMsiTIGR03594, GTPase_EngA, 1 hit
    TIGR00231, small_GTP, 2 hits
    PROSITEiView protein in PROSITE
    PS51712, G_ENGA, 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 nameiDER_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: P0A6P5
    Secondary accession number(s): P77254, Q8X4Y1
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: May 10, 2005
    Last modified: October 7, 2020
    This is version 125 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, 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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