GenePage for the dosP gene of Escherichia coli K-12

Primary Gene Name: dosP
EcoGene Accession Number: EG13792
K-12 Gene Accession Number: ECK1483
MG1655 Gene Identifier: b1489
Gene Name Mnemonic: Direct oxygen sensor phosphodiesterase
Alternate Gene Symbols: dos; yddU
Description: Heme-regulated oxygen sensor, c-di-GMP phosphodiesterase; biofilm regulator; may have weak cAMP PDE activity; cold- and stationary phase-inducible; dimeric; dual domain protein; defective cyclase domain
  # bp Upstream # bp Downstream
MW: 90260.38 ---------799 aa Pre-Run BlastP UniProt
Pre-Run BlastP NR+Env
Left End: 1563334
Left Intergenic Region

Name: ddpX_dosP

Length: 257 bp gap

Orientation: Codirectional-

Left_end: 1563077

Right_end: 1563333

Centisome: 33.68

Genomic Address
Counterclockwise
Minute or Centisome (%) = 33.68
Right End: 1565733
Right Intergenic Region

Name: dosP_dosC

Length: 24 bp gap

Orientation: Codirectional-

Left_end: 1565734

Right_end: 1565757

Centisome: 33.73

DosCP regulates biofilm formation through the oxygen-dependent activation of the csgBAC operon (Tagliabue, 2010a). DosCP may constitute a cyclic-di-GMP synthesis/degradation module (Mendez-Ortiz, 2006; Tuckerman, 2009). Dos has been renamed as DosP (Tuckerman, 2009). The EAL domain of DosP has been shown to be a c-di-GMP-specific phosphodiesterase and does not have significant cAMP phosphodiesterase activity, in contrast to an earlier report (Sasakura, 2002; Schmidt, 2005). cAMP hydrolysis by full length DosP found by Sasakura (2002) is three orders of magnitude slower than the rate of c-di-GMP hydrolysis, may not be physiologically relevant, and may be due to the use of 2'-O-anthraniloyl-cAMP instead of cAMP as substrate (Schmidt, 2005). Contrary to previous reports of a DosP tetramer (based on gel filtration), full-length DosP is a dimer in solution (Lechauve, 2009). Redox changes in the bound heme result in global 3D structural alterations; this "scissor-type" subunit movement aids in catalytic control. DosP contains 2 N-terminal heme binding PAS domains, a central defective GGDEF domain, and a C-terminal EAL domain. The start codon might be 8 codons upstream. dosP expression is elevated under aerobic conditions where it is partially responsible for cAMP degradation. The heme binding domain has been referred to as DosH. Asp40 of DosP is involved in the electronic structure of the haem iron and redox-dependent catalytic control of the PDE domain because mutations in Asp40 result in lack of catalytic activity. A dosP mutant is reported to have elevated cAMP under aerobic conditions, but this may be an indirect effect or it may reflect a physiologically relevant cAMP PDE activity in vivo. dosCP is an operon and DosCP is a protein complex (Tuckerman, 2009).

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BamHI EcoRI HindIII