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Entry version 167 (11 Dec 2019)
Sequence version 4 (04 Dec 2007)
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Protein

Oxygen sensor protein DosP

Gene

dosP

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

Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP (PubMed:15995192) but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate (PubMed:11970957). Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits.3 Publications

Miscellaneous

Binds O2 with a dissociation constant of about 74 µM.

<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

Protein has several cofactor binding sites:

<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

Has c-di-GMP PDE activity in both Fe2+ and Fe3+-bound forms; this activity is increased 6-7 fold by binding of O2 and CO (PubMed:15995192) and NO (PubMed:17535805). Has cAMP PDE activity only when the heme is in the Fe2+ form. cAMP PDE activity is inhibited by oxidation of the heme iron and by binding of external ligands such as CO and NO. Also strongly inhibited by etazolate hydrochloride, a selective cAMP PDE inhibitor. PDE activity is inhibited in the absence of oxygen.3 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

For the EAL domain, residues 532-799.1 Publication
  1. KM=36 µM for c-di-GMP

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi69Iron (heme proximal ligand)1
    Metal bindingi87Iron (heme distal ligand)1

    <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

    <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 functionHydrolase
    Biological processSensory transduction, Transcription, Transcription regulation
    Ligandc-di-GMP, Heme, Iron, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:G6783-MONOMER
    ECOL316407:JW1484-MONOMER
    MetaCyc:G6783-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P76129

    <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:
    Oxygen sensor protein DosP (EC:3.1.4.52)
    Alternative name(s):
    Direct oxygen-sensing phosphodiesterase
    Short name:
    Direct oxygen sensor protein
    Ec DOS
    Heme-regulated cyclic di-GMP phosphodiesterase
    <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:dosP
    Synonyms:dos, pdeO1 Publication, yddU
    Ordered Locus Names:b1489, JW1484
    <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 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>Mutagenesisi69H → A or G: Loss of heme binding. 2 Publications1
    Mutagenesisi75H → A or G: No loss of heme binding. 1 Publication1
    Mutagenesisi87M → A or I: Ferrous heme iron changes from an exclusively hexacoordinate low-spin form to an exclusively pentacoordinate high-spin form. Ferric heme iron remains hexacoordinate but becomes a mixture of high and low spin. Increases c-di-GMP PDE activity 7-fold in absence of O(2), CO or NO, no additional increase upon addition of gases (M-A only). 3 Publications1
    Mutagenesisi87M → H: No change in heme coordination; increases c-di-GMP PDE activity 2-fold in absence of O(2), CO or NO, and 2-fold more upon addition of gases. 3 Publications1
    Mutagenesisi89R → A, E or I: The Fe(2+)-O(2) form loses c-di-GMP PDE activity, due to reduced O(2) affinity and/or increased auto-oxidation. NO and CO forms are less affected. 2 Publications1
    Mutagenesisi91L → F: Alters O(2) binding, increases auto-oxidation. 1 Publication1
    Mutagenesisi91L → T: Increases auto-oxidation. 1 Publication1
    Mutagenesisi107L → F: Significantly reduces heme-binding affinity; increases auto-oxidation. 1 Publication1
    Mutagenesisi107L → T: Increases auto-oxidation. 1 Publication1
    Mutagenesisi582H → A: Loss of cAMP PDE activity. 1 Publication1
    Mutagenesisi586H → A: Loss of cAMP PDE 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_00000799821 – 799Oxygen sensor protein DosPAdd BLAST799

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    The heme distal ligand is coordinated by Met-87 in the active Fe2+ (ferrous) form, by O2 in the O2-bound form and by H2O in the inactive Fe3+ (ferric) form.

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P76129

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

    More...
    PaxDbi
    P76129

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P76129

    <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

    Expressed in the late exponential growth phase and at higher levels in the stationary phase. A member of the dosCP operon. Expression is RpoS dependent and is higher at 28 degrees Celsius than at 37 degrees Celsius.2 Publications

    <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 (PubMed:19864414); has been previously suggested to be a homotetramer based on size exclusion chromatography (PubMed:11970957).

    Forms a complex with DosC.

    3 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4259419, 16 interactors
    850182, 1 interactor

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-3982 dosPC diguanylate cyclase/c-di-GMP phosphodiesterase complex

    Protein interaction database and analysis system

    More...
    IntActi
    P76129, 3 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b1489

    <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

    1799
    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
    P76129

    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
    P76129

    <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>Domaini10 – 81PAS 1PROSITE-ProRule annotationAdd BLAST72
    Domaini134 – 207PAS 2PROSITE-ProRule annotationAdd BLAST74
    Domaini208 – 260PACPROSITE-ProRule annotationAdd BLAST53
    Domaini402 – 532GGDEFPROSITE-ProRule annotationAdd BLAST131
    Domaini541 – 795EALPROSITE-ProRule annotationAdd BLAST255

    <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 EAL domain (residues 532 to 799) is a cyclic dinucleotide di-GMP (c-di-GMP) PDE hydrolyzing c-di-GMP to 5'pGpG; it has no activity on cAMP.1 Publication
    Binding of an external ligand to the heme located in the N-terminal sensory domain displaces the distal heme ligand from Met-87 to the ligand and triggers a conformational change that regulates the activity of the C-terminal catalytic domain.
    The heme-PAS domain (residues 1-139) forms homodimers.

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105BZU Bacteria
    COG2199 LUCA
    COG2200 LUCA
    COG2202 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000136246

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P76129

    KEGG Orthology (KO)

    More...
    KOi
    K13243

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P76129

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01948 EAL, 1 hit
    cd01949 GGDEF, 1 hit
    cd00130 PAS, 2 hits

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.20.20.450, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR012226 Diguanyl_cyclase/Pdiesterase
    IPR001633 EAL_dom
    IPR035919 EAL_sf
    IPR000160 GGDEF_dom
    IPR029787 Nucleotide_cyclase
    IPR001610 PAC
    IPR000014 PAS
    IPR000700 PAS-assoc_C
    IPR035965 PAS-like_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00563 EAL, 1 hit
    PF00990 GGDEF, 1 hit
    PF13426 PAS_9, 2 hits

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF005925 Dos, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00052 EAL, 1 hit
    SM00267 GGDEF, 1 hit
    SM00086 PAC, 2 hits
    SM00091 PAS, 2 hits

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF141868 SSF141868, 1 hit
    SSF55073 SSF55073, 1 hit
    SSF55785 SSF55785, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00254 GGDEF, 1 hit
    TIGR00229 sensory_box, 2 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50883 EAL, 1 hit
    PS50887 GGDEF, 1 hit
    PS50113 PAC, 1 hit
    PS50112 PAS, 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.

    P76129-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKLTDADNAA DGIFFPALEQ NMMGAVLINE NDEVMFFNPA AEKLWGYKRE
    60 70 80 90 100
    EVIGNNIDML IPRDLRPAHP EYIRHNREGG KARVEGMSRE LQLEKKDGSK
    110 120 130 140 150
    IWTRFALSKV SAEGKVYYLA LVRDASVEMA QKEQTRQLII AVDHLDRPVI
    160 170 180 190 200
    VLDPERHIVQ CNRAFTEMFG YCISEASGMQ PDTLLNIPEF PADNRIRLQQ
    210 220 230 240 250
    LLWKTARDQD EFLLLTRTGE KIWIKASISP VYDVLAHLQN LVMTFSDITE
    260 270 280 290 300
    ERQIRQLEGN ILAAMCSSPP FHEMGEIICR NIESVLNESH VSLFALRNGM
    310 320 330 340 350
    PIHWASSSHG AEIQNAQSWS ATIRQRDGAP AGILQIKTSS GAETSAFIER
    360 370 380 390 400
    VADISQHMAA LALEQEKSRQ HIEQLIQFDP MTGLPNRNNL HNYLDDLVDK
    410 420 430 440 450
    AVSPVVYLIG VDHIQDVIDS LGYAWADQAL LEVVNRFREK LKPDQYLCRI
    460 470 480 490 500
    EGTQFVLVSL ENDVSNITQI ADELRNVVSK PIMIDDKPFP LTLSIGISYD
    510 520 530 540 550
    LGKNRDYLLS TAHNAMDYIR KNGGNGWQFF SPAMNEMVKE RLVLGAALKE
    560 570 580 590 600
    AISNNQLKLV YQPQIFAETG ELYGIEALAR WHDPLHGHVP PSRFIPLAEE
    610 620 630 640 650
    IGEIENIGRW VIAEACRQLA EWRSQNIHIP ALSVNLSALH FRSNQLPNQV
    660 670 680 690 700
    SDAMHAWGID GHQLTVEITE SMMMEHDTEI FKRIQILRDM GVGLSVDDFG
    710 720 730 740 750
    TGFSGLSRLV SLPVTEIKID KSFVDRCLTE KRILALLEAI TSIGQSLNLT
    760 770 780 790
    VVAEGVETKE QFEMLRKIHC RVIQGYFFSR PLPAEEIPGW MSSVLPLKI
    Length:799
    Mass (Da):90,260
    Last modified:December 4, 2007 - v4
    <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:i4CE770D2A6B39D5F
    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: AAC74562.2
    AP009048 Genomic DNA Translation: BAA15154.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    D64902

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416006.4, NC_000913.3
    WP_001360132.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74562; AAC74562; b1489
    BAA15154; BAA15154; BAA15154

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    945815

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1484
    eco:b1489

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.778

    <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: AAC74562.2
    AP009048 Genomic DNA Translation: BAA15154.1
    PIRiD64902
    RefSeqiNP_416006.4, NC_000913.3
    WP_001360132.1, NZ_LN832404.1

    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
    1S66X-ray1.80L/U8-126[»]
    1S67X-ray1.50L/U8-126[»]
    1V9YX-ray1.32A/B1-139[»]
    1V9ZX-ray1.90A/B1-139[»]
    1VB6X-ray1.56A/B1-139[»]
    4HU3X-ray3.30A529-799[»]
    4HU4X-ray2.40A/B529-799[»]
    SMRiP76129
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4259419, 16 interactors
    850182, 1 interactor
    ComplexPortaliCPX-3982 dosPC diguanylate cyclase/c-di-GMP phosphodiesterase complex
    IntActiP76129, 3 interactors
    STRINGi511145.b1489

    Proteomic databases

    jPOSTiP76129
    PaxDbiP76129
    PRIDEiP76129

    Genome annotation databases

    EnsemblBacteriaiAAC74562; AAC74562; b1489
    BAA15154; BAA15154; BAA15154
    GeneIDi945815
    KEGGiecj:JW1484
    eco:b1489
    PATRICifig|1411691.4.peg.778

    Organism-specific databases

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

    More...
    EchoBASEi
    EB3553

    Phylogenomic databases

    eggNOGiENOG4105BZU Bacteria
    COG2199 LUCA
    COG2200 LUCA
    COG2202 LUCA
    HOGENOMiHOG000136246
    InParanoidiP76129
    KOiK13243
    PhylomeDBiP76129

    Enzyme and pathway databases

    BioCyciEcoCyc:G6783-MONOMER
    ECOL316407:JW1484-MONOMER
    MetaCyc:G6783-MONOMER
    SABIO-RKiP76129

    Miscellaneous databases

    EvolutionaryTraceiP76129

    Protein Ontology

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    PROi
    PR:P76129

    Family and domain databases

    CDDicd01948 EAL, 1 hit
    cd01949 GGDEF, 1 hit
    cd00130 PAS, 2 hits
    Gene3Di3.20.20.450, 1 hit
    InterProiView protein in InterPro
    IPR012226 Diguanyl_cyclase/Pdiesterase
    IPR001633 EAL_dom
    IPR035919 EAL_sf
    IPR000160 GGDEF_dom
    IPR029787 Nucleotide_cyclase
    IPR001610 PAC
    IPR000014 PAS
    IPR000700 PAS-assoc_C
    IPR035965 PAS-like_dom_sf
    PfamiView protein in Pfam
    PF00563 EAL, 1 hit
    PF00990 GGDEF, 1 hit
    PF13426 PAS_9, 2 hits
    PIRSFiPIRSF005925 Dos, 1 hit
    SMARTiView protein in SMART
    SM00052 EAL, 1 hit
    SM00267 GGDEF, 1 hit
    SM00086 PAC, 2 hits
    SM00091 PAS, 2 hits
    SUPFAMiSSF141868 SSF141868, 1 hit
    SSF55073 SSF55073, 1 hit
    SSF55785 SSF55785, 2 hits
    TIGRFAMsiTIGR00254 GGDEF, 1 hit
    TIGR00229 sensory_box, 2 hits
    PROSITEiView protein in PROSITE
    PS50883 EAL, 1 hit
    PS50887 GGDEF, 1 hit
    PS50113 PAC, 1 hit
    PS50112 PAS, 2 hits

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <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 nameiDOSP_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: P76129
    Secondary accession number(s): P76872, P77708
    <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: December 15, 1998
    Last sequence update: December 4, 2007
    Last modified: December 11, 2019
    This is version 167 of the entry and version 4 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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