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Protein

Diguanylate cyclase DosC

Gene

dosC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

Catalytic activityi

2 GTP = 2 diphosphate + cyclic di-3',5'-guanylate.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • hemeNote: Binds 1 heme group per subunit. The Fe2+ state binds O(2) and CO while the Fe3+ state can bind CN- and imidazole.
  • Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

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.

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

      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
      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
      Metal bindingi98Iron (heme proximal ligand)1
      Metal bindingi333MagnesiumBy similarity1
      Sitei338Transition state stabilizerSequence analysis1
      Binding sitei341SubstrateBy similarity1
      Binding sitei350SubstrateBy similarity1
      Active sitei376Proton acceptorSequence analysis1
      Metal bindingi376MagnesiumBy similarity1

      GO - Molecular functioni

      GO - Biological processi

      Keywordsi

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

      Enzyme and pathway databases

      BioCyciEcoCyc:G6784-MONOMER
      MetaCyc:G6784-MONOMER
      BRENDAi2.7.7.65 2026
      UniPathwayi
      UPA00599

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Diguanylate cyclase DosC (EC:2.7.7.65)
      Short name:
      DGC
      Alternative name(s):
      Direct oxygen-sensing cyclase
      Gene namesi
      Name:dosC
      Synonyms:dgcO1 Publication, yddV
      Ordered Locus Names:b1490, JW5241
      OrganismiEscherichia coli (strain K12)
      Taxonomic identifieri83333 [NCBI]
      Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
      Proteomesi
      • UP000000318 Componenti: Chromosome
      • UP000000625 Componenti: Chromosome

      Organism-specific databases

      EcoGeneiEG13793 dosC

      Subcellular locationi

      GO - Cellular componenti

      Pathology & Biotechi

      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
      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

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      ChainiPRO_00002013211 – 460Diguanylate cyclase DosCAdd BLAST460

      Proteomic databases

      EPDiP0AA89
      PaxDbiP0AA89
      PRIDEiP0AA89

      Expressioni

      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

      Interactioni

      Subunit structurei

      Forms a complex with DosP.

      Protein-protein interaction databases

      BioGridi4262162, 6 interactors
      STRINGi316385.ECDH10B_1621

      Structurei

      Secondary structure

      1460
      Legend: HelixTurnBeta strandPDB Structure known for this area
      Show more details

      3D structure databases

      ProteinModelPortaliP0AA89
      SMRiP0AA89
      ModBaseiSearch...
      MobiDBiSearch...

      Family & Domainsi

      Domains and Repeats

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Domaini325 – 458GGDEFPROSITE-ProRule annotationAdd BLAST134

      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

      eggNOGiENOG4105BZU Bacteria
      ENOG410XNMH LUCA
      HOGENOMiHOG000006777
      InParanoidiP0AA89
      KOiK13069

      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

      Sequencei

      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
      Checksum:i79168311553E61C3
      GO

      Sequence cautioni

      The sequence BAA15155 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

      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

      Genome annotation databases

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

      Similar proteinsi

      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
      PaxDbiP0AA89
      PRIDEiP0AA89

      Protocols and materials databases

      DNASUi945835
      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

      EchoBASEiEB3554
      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

      PROiPR: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
      ProtoNetiSearch...

      Entry informationi

      Entry nameiDOSC_ECOLI
      AccessioniPrimary (citable) accession number: P0AA89
      Secondary accession number(s): P77793
      Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 13, 2005
      Last sequence update: September 13, 2005
      Last modified: November 7, 2018
      This is version 108 of the entry and version 1 of the sequence. See complete history.
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programProkaryotic Protein Annotation Program

      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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