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Protein

Diguanylate cyclase DosC

Gene

dosC

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

Globin-coupled heme-based oxygen sensor protein displaying diguanylate cyclase (DGC) activity in response to oxygen availability. Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules. Is involved in the modulation of intracellular c-di-GMP levels, in association with DosP which catalyzes the degradation of c-di-GMP (PDE activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. DosC regulates biofilm formation through the oxygen-dependent activation of the csgBAC operon, which encodes curli structural subunits, while not affecting the expression of the regulatory operon csgDEFG. DosC, but not the other DGCs in E.coli, also promotes the production of the exopolysaccharide poly-N-acetylglucosamine (PNAG) through up-regulation of the expression of the PNAG biosynthetic pgaABCD operon, independently of CsrA.
Overexpression leads to an increased level of c-di-GMP, which leads to changes in the cell surface, to abnormal cell division, increased biofilm formation and decreased swimming (the latter 2 in strain W3110). In a strain able to produce cellulose (strain TOB1, a fecal isolate) overexpression leads to an increase in cellulose production.

<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 ‘Function’ 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

Activity depends on O2-binding and heme redox state: the Fe(III), Fe(II)-O2, and Fe(II)-CO complexes of DosC are active forms, whereas Fe(II) and Fe(II)-NO complexes are inactive forms.1 Publication

Redox potential

E0 is -17 mV.

<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

The Fe(III), Fe(II)-O2, and Fe(II)-CO complexes of DosC display DGC activity with turnover numbers of 0.066, 0.022, and 0.022 min(-1), respectively. The DGC reaction catalyzed by DosC is the rate-determining step for c-di-GMP homeostasis. Binds O2, CO, cyanide and imidazole with a dissociation constant of 14 µM, 0.095 µM, 4.7 µM and 0.055 µM, respectively.1 Publication

      <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 3',5'-cyclic di-GMP biosynthesis

      This protein is involved in the pathway 3',5'-cyclic di-GMP biosynthesis, which is part of Purine metabolism.
      View all proteins of this organism that are known to be involved in the pathway 3',5'-cyclic di-GMP biosynthesis and in Purine metabolism.

      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>Sitei43Involved in oxygen binding and important for the stability of the Fe(II)-O(2) complex1
      Sitei60Important for oxygen binding and stability of the Fe(II)-O(2) complex1
      Sitei65Critical for restricting water access to the heme distal side to avoid rapid autoxidation1
      <p>This subsection of the ‘Function’ 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 bindingi98Iron (heme proximal ligand)1
      Metal bindingi333MagnesiumBy similarity1
      Sitei338Transition state stabilizerSequence analysis1
      <p>This subsection of the ‘Function’ 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 sitei341SubstrateBy similarity1
      Binding sitei350SubstrateBy similarity1
      <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei376Proton acceptorSequence analysis1
      Metal bindingi376MagnesiumBy similarity1

      <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 functionTransferase
      Biological processTranscription, Transcription regulation
      LigandGTP-binding, Heme, Iron, Magnesium, Metal-binding, Nucleotide-binding

      Enzyme and pathway databases

      BioCyc Collection of Pathway/Genome Databases

      More...
      BioCyci
      EcoCyc:G6784-MONOMER
      MetaCyc:G6784-MONOMER

      BRENDA Comprehensive Enzyme Information System

      More...
      BRENDAi
      2.7.7.65 2026

      UniPathway: a resource for the exploration and annotation of metabolic pathways

      More...
      UniPathwayi
      UPA00599

      <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:
      Diguanylate cyclase DosC (EC:2.7.7.65)
      Short name:
      DGC
      Alternative name(s):
      Direct oxygen-sensing cyclase
      <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:dosC
      Synonyms:dgcO1 Publication, yddV
      Ordered Locus Names:b1490, JW5241
      <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
      EG13793 dosC

      <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

      Disruption results in a 2.5-fold reduction in surface adhesion, a 3.5-fold reduction in biofilm formation, a large reduction in curli production, a drastic decrease in csgB expression (400-fold reduction in aerobic growth) and in an approximately 3.5-fold reduction in pgaA transcript levels in comparison with wild-type. Disruption partially suppresses the reduced motility of a pdeH disruption; concomitant disruption of dosC, dgcE, dgcQ and dgcN completely restores motility, suggesting these 4 genes, together with the c-di-GMP phosphodiesterase PdeH, form a network that regulates cell motility by altering levels of c-di-GMP.3 Publications

      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>Mutagenesisi43Y → A or L: Same biofilm formation activity as wild-type. Large decrease in O(2) affinity. 1 Publication1
      Mutagenesisi43Y → F or W: Same biofilm formation activity as wild-type. Markedly enhanced O(2) dissociation but not association rate constants. Highly enhanced autoxidation rate constant. 1 Publication1
      Mutagenesisi60Q → A or E: Same biofilm formation activity as wild-type. Enhanced O(2) dissociation but not association rate constants. Enhanced autoxidation rate constant. 1 Publication1
      Mutagenesisi60Q → L: Same biofilm formation activity as wild-type. 5-fold reduction in O(2) dissociation rate constant. Significant decrease in the autoxidation rate constant. 1 Publication1
      Mutagenesisi65L → G or T: Enhanced autoxidation rate constant. Markedly enhanced O(2) association rate constant. 1 Publication1
      Mutagenesisi65L → M or Q: Enhanced autoxidation rate constant. Decrease in O(2) association rate constant. 1 Publication1
      Mutagenesisi98H → A: Same biofilm formation activity as wild-type. Loss of heme-binding ability. 1 Publication1
      Mutagenesisi223H → A: Same biofilm formation activity as wild-type. 1 Publication1
      Mutagenesisi365R → A: Same biofilm formation activity as wild-type. 1 Publication1
      Mutagenesisi368D → A: Lacks biofilm formation activity, and thus is probably devoid of diguanylate cyclase activity. 1 Publication1
      Mutagenesisi376 – 377DE → AA: Loss of DGC activity. Stimulation of PNAG production and activation of pgaABCD expression are abolished. 1 Publication2
      Mutagenesisi376D → A: Lacks biofilm formation activity, and thus is probably devoid of diguanylate cyclase activity. 1 Publication1
      Mutagenesisi377E → A: Lacks biofilm formation activity, and thus is probably devoid of diguanylate cyclase 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_00002013211 – 460Diguanylate cyclase DosCAdd BLAST460

      Proteomic databases

      Encyclopedia of Proteome Dynamics

      More...
      EPDi
      P0AA89

      jPOST - Japan Proteome Standard Repository/Database

      More...
      jPOSTi
      P0AA89

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

      More...
      PaxDbi
      P0AA89

      PRoteomics IDEntifications database

      More...
      PRIDEi
      P0AA89

      <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

      By RpoS in the late exponential growth phase and upon entry into stationary phase. Expression is higher at 28 than 37 degrees Celsius. In rich medium DosC and DgcM are the major RpoS-dependent GGDEF-domain containing proteins in the cell, whereas in minimal medium it is the major RpoS-dependent GGDEF-domain containing protein. Highly expressed on solid medium. A member of the dosCP operon.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

      Forms a complex with DosP.

      Protein-protein interaction databases

      The Biological General Repository for Interaction Datasets (BioGrid)

      More...
      BioGridi
      4262162, 6 interactors

      STRING: functional protein association networks

      More...
      STRINGi
      316385.ECDH10B_1621

      <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

      1460
      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
      4ZVAX-ray2.00A/B8-170[»]
      4ZVBX-ray2.40A/B/C/D1-155[»]
      4ZVCX-ray1.50A/B173-298[»]
      4ZVDX-ray1.90A/B173-298[»]
      4ZVEX-ray1.20A297-460[»]
      4ZVFX-ray1.15A297-460[»]
      4ZVGX-ray2.20A/B297-460[»]
      4ZVHX-ray3.30A/B297-460[»]

      Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

      More...
      ProteinModelPortali
      P0AA89

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

      More...
      SMRi
      P0AA89

      Database of comparative protein structure models

      More...
      ModBasei
      Search...

      MobiDB: a database of protein disorder and mobility annotations

      More...
      MobiDBi
      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>Domaini325 – 458GGDEFPROSITE-ProRule annotationAdd BLAST134

      <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

      Is composed of an N-terminal sensory globin-fold domain that binds heme and oxygen, and a C-terminal GGDEF diguanylate cyclase domain.1 Publication

      Phylogenomic databases

      evolutionary genealogy of genes: Non-supervised Orthologous Groups

      More...
      eggNOGi
      ENOG4105BZU Bacteria
      ENOG410XNMH LUCA

      The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

      More...
      HOGENOMi
      HOG000006777

      InParanoid: Eukaryotic Ortholog Groups

      More...
      InParanoidi
      P0AA89

      KEGG Orthology (KO)

      More...
      KOi
      K13069

      Family and domain databases

      Conserved Domains Database

      More...
      CDDi
      cd01949 GGDEF, 1 hit
      cd14757 GS_EcDosC-like_GGDEF, 1 hit

      Gene3D Structural and Functional Annotation of Protein Families

      More...
      Gene3Di
      1.10.490.10, 1 hit

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR039435 DosC_GS
      IPR000160 GGDEF_dom
      IPR009050 Globin-like_sf
      IPR012292 Globin/Proto
      IPR029787 Nucleotide_cyclase

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF00990 GGDEF, 1 hit

      Simple Modular Architecture Research Tool; a protein domain database

      More...
      SMARTi
      View protein in SMART
      SM00267 GGDEF, 1 hit

      Superfamily database of structural and functional annotation

      More...
      SUPFAMi
      SSF46458 SSF46458, 1 hit
      SSF55073 SSF55073, 1 hit

      TIGRFAMs; a protein family database

      More...
      TIGRFAMsi
      TIGR00254 GGDEF, 1 hit

      PROSITE; a protein domain and family database

      More...
      PROSITEi
      View protein in PROSITE
      PS50887 GGDEF, 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.

      P0AA89-1 [UniParc]FASTAAdd to basket
      « Hide
              10         20         30         40         50
      MEMYFKRMKD EWTGLVEQAD PPIRAKAAEI AVAHAHYLSI EFYRIVRIDP
      60 70 80 90 100
      HAEEFLSNEQ VERQLKSAME RWIINVLSAQ VDDVERLIQI QHTVAEVHAR
      110 120 130 140 150
      IGIPVEIVEM GFRVLKKILY PVIFSSDYSA AEKLQVYHFS INSIDIAMEV
      160 170 180 190 200
      MTRAFTFSDS SASKEDENYR IFSLLENAEE EKERQIASIL SWEIDIIYKI
      210 220 230 240 250
      LLDSDLGSSL PLSQADFGLW FNHKGRHYFS GIAEVGHISR LIQDFDGIFN
      260 270 280 290 300
      QTMRNTRNLN NRSLRVKFLL QIRNTVSQII TLLRELFEEV SRHEVGMDVL
      310 320 330 340 350
      TKLLNRRFLP TIFKREIAHA NRTGTPLSVL IIDVDKFKEI NDTWGHNTGD
      360 370 380 390 400
      EILRKVSQAF YDNVRSSDYV FRYGGDEFII VLTEASENET LRTAERIRSR
      410 420 430 440 450
      VEKTKLKAAN GEDIALSLSI GAAMFNGHPD YERLIQIADE ALYIAKRRGR
      460
      NRVELWKASL
      Length:460
      Mass (Da):53,178
      Last modified:September 13, 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:i79168311553E61C3
      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 BAA15155 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.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
      U00096 Genomic DNA Translation: AAC74563.3
      AP009048 Genomic DNA Translation: BAA15155.2 Different initiation.

      Protein sequence database of the Protein Information Resource

      More...
      PIRi
      E64902

      NCBI Reference Sequences

      More...
      RefSeqi
      NP_416007.3, NC_000913.3
      WP_000426292.1, NZ_LN832404.1

      Genome annotation databases

      Ensembl bacterial and archaeal genome annotation project

      More...
      EnsemblBacteriai
      AAC74563; AAC74563; b1490
      BAA15155; BAA15155; BAA15155

      Database of genes from NCBI RefSeq genomes

      More...
      GeneIDi
      945835

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...
      KEGGi
      ecj:JW5241
      eco:b1490

      Pathosystems Resource Integration Center (PATRIC)

      More...
      PATRICi
      fig|1411691.4.peg.777

      <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: AAC74563.3
      AP009048 Genomic DNA Translation: BAA15155.2 Different initiation.
      PIRiE64902
      RefSeqiNP_416007.3, NC_000913.3
      WP_000426292.1, NZ_LN832404.1

      3D structure databases

      Select the link destinations:
      PDBei
      RCSB PDBi
      PDBji
      Links Updated
      PDB entryMethodResolution (Å)ChainPositionsPDBsum
      4ZVAX-ray2.00A/B8-170[»]
      4ZVBX-ray2.40A/B/C/D1-155[»]
      4ZVCX-ray1.50A/B173-298[»]
      4ZVDX-ray1.90A/B173-298[»]
      4ZVEX-ray1.20A297-460[»]
      4ZVFX-ray1.15A297-460[»]
      4ZVGX-ray2.20A/B297-460[»]
      4ZVHX-ray3.30A/B297-460[»]
      ProteinModelPortaliP0AA89
      SMRiP0AA89
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      BioGridi4262162, 6 interactors
      STRINGi316385.ECDH10B_1621

      Proteomic databases

      EPDiP0AA89
      jPOSTiP0AA89
      PaxDbiP0AA89
      PRIDEiP0AA89

      Protocols and materials databases

      The DNASU plasmid repository

      More...
      DNASUi
      945835
      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      EnsemblBacteriaiAAC74563; AAC74563; b1490
      BAA15155; BAA15155; BAA15155
      GeneIDi945835
      KEGGiecj:JW5241
      eco:b1490
      PATRICifig|1411691.4.peg.777

      Organism-specific databases

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

      More...
      EchoBASEi
      EB3554
      EcoGeneiEG13793 dosC

      Phylogenomic databases

      eggNOGiENOG4105BZU Bacteria
      ENOG410XNMH LUCA
      HOGENOMiHOG000006777
      InParanoidiP0AA89
      KOiK13069

      Enzyme and pathway databases

      UniPathwayi
      UPA00599

      BioCyciEcoCyc:G6784-MONOMER
      MetaCyc:G6784-MONOMER
      BRENDAi2.7.7.65 2026

      Miscellaneous databases

      Protein Ontology

      More...
      PROi
      PR:P0AA89

      Family and domain databases

      CDDicd01949 GGDEF, 1 hit
      cd14757 GS_EcDosC-like_GGDEF, 1 hit
      Gene3Di1.10.490.10, 1 hit
      InterProiView protein in InterPro
      IPR039435 DosC_GS
      IPR000160 GGDEF_dom
      IPR009050 Globin-like_sf
      IPR012292 Globin/Proto
      IPR029787 Nucleotide_cyclase
      PfamiView protein in Pfam
      PF00990 GGDEF, 1 hit
      SMARTiView protein in SMART
      SM00267 GGDEF, 1 hit
      SUPFAMiSSF46458 SSF46458, 1 hit
      SSF55073 SSF55073, 1 hit
      TIGRFAMsiTIGR00254 GGDEF, 1 hit
      PROSITEiView protein in PROSITE
      PS50887 GGDEF, 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 nameiDOSC_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: P0AA89
      Secondary accession number(s): P77793
      <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: September 13, 2005
      Last sequence update: September 13, 2005
      Last modified: January 16, 2019
      This is version 110 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. PATHWAY comments
        Index of metabolic and biosynthesis pathways
      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
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