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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-Experimental evidence at protein leveli

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

Catalytic activityi

Cyclic di-3',5'-guanylate + H2O = 5'-phosphoguanylyl(3'->5')guanosine.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme 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

Kineticsi

For the EAL domain, residues 532-799.1 Publication

  1. KM=36 µM for c-di-GMP

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi69 – 691Iron (heme proximal ligand)
    Metal bindingi87 – 871Iron (heme distal ligand)

    GO - Molecular functioni

    • cyclic-guanylate-specific phosphodiesterase activity Source: EcoCyc
    • heme binding Source: EcoCyc
    • magnesium ion binding Source: EcoCyc
    • oxygen sensor activity Source: CACAO
    • phosphorelay sensor kinase activity Source: InterPro

    GO - Biological processi

    • regulation of transcription, DNA-templated Source: UniProtKB-KW
    • response to oxygen levels Source: EcoCyc
    • transcription, DNA-templated Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Sensory transduction, Transcription, Transcription regulation

    Keywords - Ligandi

    c-di-GMP, Heme, Iron, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:G6783-MONOMER.
    ECOL316407:JW1484-MONOMER.
    MetaCyc:G6783-MONOMER.
    SABIO-RKP76129.

    Names & Taxonomyi

    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
    Gene namesi
    Name:dosP
    Synonyms:dos, yddU
    Ordered Locus Names:b1489, JW1484
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13792. dosP.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi69 – 691H → A or G: Loss of heme binding. 2 Publications
    Mutagenesisi75 – 751H → A or G: No loss of heme binding. 1 Publication
    Mutagenesisi87 – 871M → 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 Publications
    Mutagenesisi87 – 871M → 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 Publications
    Mutagenesisi89 – 891R → 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 Publications
    Mutagenesisi91 – 911L → F: Alters O(2) binding, increases auto-oxidation. 1 Publication
    Mutagenesisi91 – 911L → T: Increases auto-oxidation. 1 Publication
    Mutagenesisi107 – 1071L → F: Significantly reduces heme-binding affinity; increases auto-oxidation. 1 Publication
    Mutagenesisi107 – 1071L → T: Increases auto-oxidation. 1 Publication
    Mutagenesisi582 – 5821H → A: Loss of cAMP PDE activity. 1 Publication
    Mutagenesisi586 – 5861H → A: Loss of cAMP PDE activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 799799Oxygen sensor protein DosPPRO_0000079982Add
    BLAST

    Post-translational modificationi

    The heme distal ligand is coordinated by Met-87 in the active Fe2+ (ferrous) form, by O2 in the O(2)-bound form and by H2O in the inactive Fe3+ (ferric) form.

    Proteomic databases

    PaxDbiP76129.

    Expressioni

    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

    Interactioni

    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

    BioGridi4259419. 16 interactions.
    IntActiP76129. 3 interactions.
    STRINGi511145.b1489.

    Structurei

    Secondary structure

    1
    799
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 196Combined sources
    Beta strandi22 – 287Combined sources
    Beta strandi32 – 376Combined sources
    Helixi39 – 457Combined sources
    Helixi49 – 513Combined sources
    Turni52 – 543Combined sources
    Helixi57 – 604Combined sources
    Helixi63 – 653Combined sources
    Turni66 – 683Combined sources
    Helixi69 – 779Combined sources
    Beta strandi90 – 945Combined sources
    Beta strandi96 – 983Combined sources
    Beta strandi100 – 11213Combined sources
    Beta strandi115 – 1239Combined sources
    Helixi544 – 5496Combined sources
    Turni552 – 5554Combined sources
    Beta strandi557 – 56913Combined sources
    Beta strandi572 – 58312Combined sources
    Turni584 – 5863Combined sources
    Beta strandi587 – 5893Combined sources
    Helixi591 – 5944Combined sources
    Turni595 – 5973Combined sources
    Helixi607 – 62317Combined sources
    Beta strandi632 – 6365Combined sources
    Turni637 – 6404Combined sources
    Helixi648 – 6569Combined sources
    Beta strandi657 – 6593Combined sources
    Beta strandi664 – 6685Combined sources
    Helixi670 – 6723Combined sources
    Turni675 – 6773Combined sources
    Helixi680 – 6889Combined sources
    Turni689 – 6913Combined sources
    Beta strandi693 – 6964Combined sources
    Helixi703 – 7075Combined sources
    Turni708 – 7114Combined sources
    Beta strandi715 – 7195Combined sources
    Helixi721 – 7299Combined sources
    Helixi731 – 74616Combined sources
    Beta strandi750 – 7545Combined sources
    Helixi759 – 7679Combined sources
    Beta strandi772 – 7754Combined sources
    Turni776 – 7783Combined sources
    Helixi784 – 7863Combined sources
    Helixi787 – 7937Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP76129.
    SMRiP76129. Positions 8-126, 378-799.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP76129.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 8172PAS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini134 – 20774PAS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini208 – 26053PACPROSITE-ProRule annotationAdd
    BLAST
    Domaini402 – 532131GGDEFPROSITE-ProRule annotationAdd
    BLAST
    Domaini541 – 795255EALPROSITE-ProRule annotationAdd
    BLAST

    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.

    Sequence similaritiesi

    Contains 1 EAL domain.PROSITE-ProRule annotation
    Contains 1 GGDEF domain.PROSITE-ProRule annotation
    Contains 1 PAC (PAS-associated C-terminal) domain.PROSITE-ProRule annotation
    Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiENOG4105BZU. Bacteria.
    COG2199. LUCA.
    COG2200. LUCA.
    COG2202. LUCA.
    HOGENOMiHOG000136246.
    InParanoidiP76129.
    KOiK13243.
    OMAiCHEVERI.
    OrthoDBiEOG69GZGV.
    PhylomeDBiP76129.

    Family and domain databases

    Gene3Di3.20.20.450. 1 hit.
    InterProiIPR001633. EAL_dom.
    IPR000160. GGDEF_dom.
    IPR029787. Nucleotide_cyclase.
    IPR001610. PAC.
    IPR000014. PAS.
    IPR000700. PAS-assoc_C.
    [Graphical view]
    PfamiPF00563. EAL. 1 hit.
    PF00990. GGDEF. 1 hit.
    PF13426. PAS_9. 2 hits.
    [Graphical view]
    SMARTiSM00052. EAL. 1 hit.
    SM00267. GGDEF. 1 hit.
    SM00086. PAC. 2 hits.
    SM00091. PAS. 2 hits.
    [Graphical view]
    SUPFAMiSSF141868. SSF141868. 1 hit.
    SSF55073. SSF55073. 1 hit.
    SSF55785. SSF55785. 2 hits.
    TIGRFAMsiTIGR00254. GGDEF. 1 hit.
    TIGR00229. sensory_box. 2 hits.
    PROSITEiPS50883. EAL. 1 hit.
    PS50887. GGDEF. 1 hit.
    PS50113. PAC. 1 hit.
    PS50112. PAS. 2 hits.
    [Graphical view]

    Sequencei

    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
    Checksum:i4CE770D2A6B39D5F
    GO

    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.

    Genome annotation databases

    EnsemblBacteriaiAAC74562; AAC74562; b1489.
    BAA15154; BAA15154; BAA15154.
    GeneIDi945815.
    KEGGiecj:JW1484.
    eco:b1489.
    PATRICi32118272. VBIEscCol129921_1556.

    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP76129.
    SMRiP76129. Positions 8-126, 378-799.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259419. 16 interactions.
    IntActiP76129. 3 interactions.
    STRINGi511145.b1489.

    Proteomic databases

    PaxDbiP76129.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74562; AAC74562; b1489.
    BAA15154; BAA15154; BAA15154.
    GeneIDi945815.
    KEGGiecj:JW1484.
    eco:b1489.
    PATRICi32118272. VBIEscCol129921_1556.

    Organism-specific databases

    EchoBASEiEB3553.
    EcoGeneiEG13792. dosP.

    Phylogenomic databases

    eggNOGiENOG4105BZU. Bacteria.
    COG2199. LUCA.
    COG2200. LUCA.
    COG2202. LUCA.
    HOGENOMiHOG000136246.
    InParanoidiP76129.
    KOiK13243.
    OMAiCHEVERI.
    OrthoDBiEOG69GZGV.
    PhylomeDBiP76129.

    Enzyme and pathway databases

    BioCyciEcoCyc:G6783-MONOMER.
    ECOL316407:JW1484-MONOMER.
    MetaCyc:G6783-MONOMER.
    SABIO-RKP76129.

    Miscellaneous databases

    EvolutionaryTraceiP76129.
    PROiP76129.

    Family and domain databases

    Gene3Di3.20.20.450. 1 hit.
    InterProiIPR001633. EAL_dom.
    IPR000160. GGDEF_dom.
    IPR029787. Nucleotide_cyclase.
    IPR001610. PAC.
    IPR000014. PAS.
    IPR000700. PAS-assoc_C.
    [Graphical view]
    PfamiPF00563. EAL. 1 hit.
    PF00990. GGDEF. 1 hit.
    PF13426. PAS_9. 2 hits.
    [Graphical view]
    SMARTiSM00052. EAL. 1 hit.
    SM00267. GGDEF. 1 hit.
    SM00086. PAC. 2 hits.
    SM00091. PAS. 2 hits.
    [Graphical view]
    SUPFAMiSSF141868. SSF141868. 1 hit.
    SSF55073. SSF55073. 1 hit.
    SSF55785. SSF55785. 2 hits.
    TIGRFAMsiTIGR00254. GGDEF. 1 hit.
    TIGR00229. sensory_box. 2 hits.
    PROSITEiPS50883. EAL. 1 hit.
    PS50887. GGDEF. 1 hit.
    PS50113. PAC. 1 hit.
    PS50112. PAS. 2 hits.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor."
      Delgado-Nixon V.M., Gonzalez G., Gilles-Gonzalez M.-A.
      Biochemistry 39:2685-2691(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], HEME-BINDING.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Nature of the displaceable heme-axial residue in the EcDos protein, a heme-based sensor from Escherichia coli."
      Gonzalez G., Dioum E.M., Bertolucci C.M., Tomita T., Ikeda-Saito M., Cheesman M.R., Watmough N.J., Gilles-Gonzalez M.-A.
      Biochemistry 41:8414-8421(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF MET-87 AND ARG-89.
    6. "Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of the heme redox states and mutations at the heme-binding site on catalysis and structure."
      Sasakura Y., Hirata S., Sugiyama S., Suzuki S., Taguchi S., Watanabe M., Matsui T., Sagami I., Shimizu T.
      J. Biol. Chem. 277:23821-23827(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, HOMOTETRAMER SUBUNIT, MUTAGENESIS OF HIS-69 AND HIS-75.
      Strain: K12 / JM109 / ATCC 53323.
    7. "Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli."
      Sato A., Sasakura Y., Sugiyama S., Sagami I., Shimizu T., Mizutani Y., Kitagawa T.
      J. Biol. Chem. 277:32650-32658(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: RESONANCE RAMAN SPECTROSCOPY, MUTAGENESIS OF MET-87.
    8. "Ligand binding dynamics to the heme domain of the oxygen sensor Dos from Escherichia coli."
      Liebl U., Bouzhir-Sima L., Kiger L., Marden M.C., Lambry J.-C., Negrerie M., Vos M.H.
      Biochemistry 42:6527-6535(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSORPTION SPECTROSCOPY.
    9. "Relationships between heme incorporation, tetramer formation, and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: a study of deletion and site-directed mutants."
      Yoshimura T., Sagami I., Sasakura Y., Shimizu T.
      J. Biol. Chem. 278:53105-53111(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-69; HIS-582 AND HIS-586.
    10. "The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains."
      Schmidt A.J., Ryjenkov D.A., Gomelsky M.
      J. Bacteriol. 187:4774-4781(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE EAL DOMAIN AS A CYCLIC DINUCLEOTIDE DI-GMP PHOSPHODIESTERASE.
      Strain: K12 / MG1655 / ATCC 47076.
    11. "Phosphodiesterase activity of Ec DOS, a heme-regulated enzyme from Escherichia coli, toward 3',5'-cyclic diguanylic acid is obviously enhanced by O2 and CO binding."
      Takahashi H., Shimizu T.
      Chem. Lett. 35:970-971(2006)
      Cited for: CHARACTERIZATION OF CYCLIC DI-GMP ACTIVITY OF THE FULL-LENGTH PROTEIN.
    12. "Critical roles of Leu99 and Leu115 at the heme distal side in auto-oxidation and the redox potential of a heme-regulated phosphodiesterase from Escherichia coli."
      Yokota N., Araki Y., Kurokawa H., Ito O., Igarashi J., Shimizu T.
      FEBS J. 273:1210-1223(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LEU-91 AND LEU-107.
      Strain: K12 / JM109 / ATCC 53323.
    13. "Genome-wide transcriptional profile of Escherichia coli in response to high levels of the second messenger 3',5'-cyclic diguanylic acid."
      Mendez-Ortiz M.M., Hyodo M., Hayakawa Y., Membrillo-Hernandez J.
      J. Biol. Chem. 281:8090-8099(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: OPERON STRUCTURE.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    14. "Critical role of the heme axial ligand, Met95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward cyclic diGMP."
      Tanaka A., Takahashi H., Shimizu T.
      J. Biol. Chem. 282:21301-21307(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE OF ARG-89 IN O(2) STABILIZATION, MUTAGENESIS OF MET-87 AND ARG-89.
      Strain: K12 / JM109 / ATCC 53323.
    15. "An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control."
      Tuckerman J.R., Gonzalez G., Sousa E.H., Wan X., Saito J.A., Alam M., Gilles-Gonzalez M.A.
      Biochemistry 48:9764-9774(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH DOSC, OPERON STRUCTURE.
    16. "Heme ligand binding properties and intradimer interactions in the full-length sensor protein dos from Escherichia coli and its isolated heme domain."
      Lechauve C., Bouzhir-Sima L., Yamashita T., Marden M.C., Vos M.H., Liebl U., Kiger L.
      J. Biol. Chem. 284:36146-36159(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMER SUBUNIT.
    17. "Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli."
      Sommerfeldt N., Possling A., Becker G., Pesavento C., Tschowri N., Hengge R.
      Microbiology 155:1318-1331(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, RPOS-DEPENDENCE.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    18. "The yddV-dos operon controls biofilm formation through the regulation of genes encoding curli fibers' subunits in aerobically growing Escherichia coli."
      Tagliabue L., Maciag A., Antoniani D., Landini P.
      FEMS Immunol. Med. Microbiol. 59:477-484(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF CSGBAC EXPRESSION, INDUCTION.
      Strain: K12 / MG1655 / ATCC 47076.
    19. "Cloning, purification, crystallization and preliminary X-ray analysis of DOS heme domain, a new heme oxygen sensor in Escherichia coli."
      Park H., Suquet C., Savenkova M.I., Satterlee J.D., Kang C.
      Acta Crystallogr. D 58:1504-1506(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION OF 1-139.
      Strain: K12.
    20. "Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (Ec DosH)."
      Park H., Suquet C., Satterlee J.D., Kang C.
      Biochemistry 43:2738-2746(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 8-136 IN COMPLEX WITH AND WITHOUT O(2).
      Strain: K12.
    21. "A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor."
      Kurokawa H., Lee D.-S., Watanabe M., Sagami I., Mikami B., Raman C.S., Shimizu T.
      J. Biol. Chem. 279:20186-20193(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 1-139 IN AN ACTIVE FE(2+)-BOUND FORM, INACTIVE FE(3+)-BOUND FORM.
      Strain: K12 / JM109 / ATCC 53323.

    Entry informationi

    Entry nameiDOSP_ECOLI
    AccessioniPrimary (citable) accession number: P76129
    Secondary accession number(s): P76872, P77708
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: December 4, 2007
    Last modified: March 16, 2016
    This is version 146 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binds O2 with a dissociation constant of about 74 µM.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.