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ECOLI:DOSP

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) dosP (synonyms: dos, yddU)
Protein Name(s) Oxygen sensor protein DosP

Direct oxygen-sensing phosphodiesterase Direct oxygen sensor protein Ec DOS Heme-regulated cyclic di-GMP phosphodiesterase,

External Links
UniProt P76129
EMBL U00096
AP009048
PIR D64902
RefSeq NP_416006.4
YP_489754.1
PDB 1S66
1S67
1V9Y
1V9Z
1VB6
4HU3
4HU4
PDBsum 1S66
1S67
1V9Y
1V9Z
1VB6
4HU3
4HU4
ProteinModelPortal P76129
SMR P76129
IntAct P76129
STRING 511145.b1489
EnsemblBacteria AAC74562
BAA15154
GeneID 12930425
945815
KEGG ecj:Y75_p1465
eco:b1489
PATRIC 32118272
EchoBASE EB3553
EcoGene EG13792
eggNOG COG2202
HOGENOM HOG000136246
InParanoid P76129
KO K13243
OMA CHEVERI
OrthoDB EOG69GZGV
PhylomeDB P76129
BioCyc EcoCyc:G6783-MONOMER
ECOL316407:JW1484-MONOMER
MetaCyc:G6783-MONOMER
SABIO-RK P76129
EvolutionaryTrace P76129
PRO PR:P76129
Proteomes UP000000318
UP000000625
Genevestigator P76129
GO GO:0071111
GO:0020037
GO:0000287
GO:0019826
GO:0000155
GO:0006355
GO:0006351
Gene3D 3.20.20.450
InterPro IPR012226
IPR001633
IPR000160
IPR029787
IPR001610
IPR000014
IPR000700
Pfam PF00563
PF00990
PF13426
PIRSF PIRSF005925
SMART SM00052
SM00267
SM00086
SM00091
SUPFAM SSF141868
SSF55073
SSF55785
TIGRFAMs TIGR00254
TIGR00229
PROSITE PS50883
PS50887
PS50113
PS50112

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0019826

oxygen sensor activity

PMID:19764732[1]

ECO:0000314

F

Figure 4

complete
CACAO 4349

enables

GO:0019826

oxygen sensor activity

PMID:19764732[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0071111

cyclic-guanylate-specific phosphodiesterase activity

PMID:15995192[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0070482

response to oxygen levels

PMID:16166529[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0020037

heme binding

PMID:10704219[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:14551206[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0071111

cyclic-guanylate-specific phosphodiesterase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.4.52

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0050896

response to stimulus

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0716

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Tuckerman, JR et al. (2009) An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control. Biochemistry 48 9764-74 PubMed GONUTS page
  2. Schmidt, AJ et al. (2005) The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J. Bacteriol. 187 4774-81 PubMed GONUTS page
  3. Yoshimura-Suzuki, T et al. (2005) DOS(Ec), a heme-regulated phosphodiesterase, plays an important role in the regulation of the cyclic AMP level in Escherichia coli. J. Bacteriol. 187 6678-82 PubMed GONUTS page
  4. Delgado-Nixon, VM et al. (2000) Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor. Biochemistry 39 2685-91 PubMed GONUTS page
  5. Yoshimura, T et al. (2003) Relationships between heme incorporation, tetramer formation, and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: a study of deletion and site-directed mutants. J. Biol. Chem. 278 53105-11 PubMed GONUTS page