P77172 · PDEF_ECOLI
- ProteinCyclic di-GMP phosphodiesterase PdeF
- GenepdeF
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids747 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG. Truncated proteins consisting of the GGDEF/EAL domains (residues 319-747) or of the EAL domain alone (481-747) have c-di-GMP phosphodiesterase activity. They do not have diguanylate cyclase activity. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.
Catalytic activity
- 3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine + H+
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Mg2+, and possibly also Mn2+.
Activity regulation
Inhibited by pGpG.
pH Dependence
Optimum pH is 7.5 for the truncated enzyme.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | cyclic-guanylate-specific phosphodiesterase activity | |
Molecular Function | nucleotide binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | cellular response to anoxia | |
Biological Process | cellular response to hydrogen peroxide | |
Biological Process | regulation of single-species biofilm formation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCyclic di-GMP phosphodiesterase PdeF
- EC number
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP77172
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-14 | Periplasmic | ||||
Sequence: MKLNATYIKIRDKW | ||||||
Transmembrane | 15-36 | Helical | ||||
Sequence: WGLPLFLPSLILPIFAHINTFA | ||||||
Topological domain | 37-42 | Cytoplasmic | ||||
Sequence: HISSGE | ||||||
Transmembrane | 43-65 | Helical | ||||
Sequence: VFLFYLPLALMISMMMFFSWAAL | ||||||
Topological domain | 66-79 | Periplasmic | ||||
Sequence: PGIALGIFVRKYAE | ||||||
Transmembrane | 80-102 | Helical | ||||
Sequence: LGFYETLSLTANFIIIIILCWGG | ||||||
Topological domain | 103-128 | Cytoplasmic | ||||
Sequence: YRVFTPRRNNVSHGDTRLISQRIFWQ | ||||||
Transmembrane | 129-151 | Helical | ||||
Sequence: IVFPATLFLILFQFAAFVGLLAS | ||||||
Topological domain | 152-165 | Periplasmic | ||||
Sequence: RENLVGVMPFNLGT | ||||||
Transmembrane | 166-188 | Helical | ||||
Sequence: LINYQALLVGNLIGVPLCYFIIR | ||||||
Topological domain | 189-215 | Cytoplasmic | ||||
Sequence: VVRNPFYLRSYYSQLKQQVDAKVTKKE | ||||||
Transmembrane | 216-235 | Helical | ||||
Sequence: FALWLLALGALLLLLCMPLN | ||||||
Topological domain | 236-239 | Periplasmic | ||||
Sequence: EKST | ||||||
Transmembrane | 240-259 | Helical | ||||
Sequence: IFSTNYTLSLLLPLMMWGAM | ||||||
Topological domain | 260-265 | Cytoplasmic | ||||
Sequence: RYGYKL | ||||||
Transmembrane | 266-285 | Helical | ||||
Sequence: ISLLWAVVLMISIHSYQNYI | ||||||
Topological domain | 286-294 | Periplasmic | ||||
Sequence: PIYPGYTTQ | ||||||
Transmembrane | 295-317 | Helical | ||||
Sequence: LTITSSSYLVFSFIVNYMAVLAT | ||||||
Topological domain | 318-747 | Cytoplasmic | ||||
Sequence: RQRAVVRRIQRLAYVDPVVHLPNVRALNRALRDAPWSALCYLRIPGMEMLVKNYGIMLRIQYKQKLSHWLSPLLEPGEDVYQLSGNDLALRLNTESHQERITALDSHLKQFRFFWDGMPMQPQIGVSYCYVRSPVNHIYLLLGELNTVAELSIVTNAPENMQRRGAMYLQRELKDKVAMMNRLQQALEHNHFFLMAQPITGMRGDVYHEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQPLIDTLNEIEPIRESA |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Increased biofilm formation but a decreased tendency to sediment and aggregate. Cells are more sensitive to peroxide.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000169241 | 1-747 | Cyclic di-GMP phosphodiesterase PdeF | |||
Sequence: MKLNATYIKIRDKWWGLPLFLPSLILPIFAHINTFAHISSGEVFLFYLPLALMISMMMFFSWAALPGIALGIFVRKYAELGFYETLSLTANFIIIIILCWGGYRVFTPRRNNVSHGDTRLISQRIFWQIVFPATLFLILFQFAAFVGLLASRENLVGVMPFNLGTLINYQALLVGNLIGVPLCYFIIRVVRNPFYLRSYYSQLKQQVDAKVTKKEFALWLLALGALLLLLCMPLNEKSTIFSTNYTLSLLLPLMMWGAMRYGYKLISLLWAVVLMISIHSYQNYIPIYPGYTTQLTITSSSYLVFSFIVNYMAVLATRQRAVVRRIQRLAYVDPVVHLPNVRALNRALRDAPWSALCYLRIPGMEMLVKNYGIMLRIQYKQKLSHWLSPLLEPGEDVYQLSGNDLALRLNTESHQERITALDSHLKQFRFFWDGMPMQPQIGVSYCYVRSPVNHIYLLLGELNTVAELSIVTNAPENMQRRGAMYLQRELKDKVAMMNRLQQALEHNHFFLMAQPITGMRGDVYHEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQPLIDTLNEIEPIRESA |
Proteomic databases
Expression
Induction
Induced by FNR. Expression is highest under anaerobic conditions at 28 degrees Celsius in stationary phase.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 493-744 | EAL | ||||
Sequence: KVAMMNRLQQALEHNHFFLMAQPITGMRGDVYHEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQPLIDTLNEIEPIR |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length747
- Mass (Da)85,608
- Last updated1997-02-01 v1
- Checksum7D5E8B0E646C8EDF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U00096 EMBL· GenBank· DDBJ | AAC75556.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA16393.1 EMBL· GenBank· DDBJ | Genomic DNA |