| IED ID |
IndEnz0002012632 |
| Enzyme Type ID |
protease012632 |
| Protein Name |
cAMP-activated global transcriptional regulator Vfr
|
| Gene Name |
vfr PA0652 |
| Organism |
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Pseudomonadales
Pseudomonadaceae
Pseudomonas
Pseudomonas aeruginosa group
Pseudomonas aeruginosa
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
|
| Enzyme Sequence |
MVAITHTPKLKHLDKLLAHCHRRRYTAKSTIIYAGDRCETLFFIIKGSVTILIEDDDGREMIIGYLNSGDFFGELGLFEKEGSEQERSAWVRAKVECEVAEISYAKFRELSQQDSEILYTLGSQMADRLRKTTRKVGDLAFLDVTGRVARTLLDLCQQPDAMTHPDGMQIKITRQEIGRIVGCSREMVGRVLKSLEEQGLVHVKGKTMVVFGTR |
| Enzyme Length |
214 |
| Uniprot Accession Number |
P55222 |
| Absorption |
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| Active Site |
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| Activity Regulation |
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| Binding Site |
BINDING 179; /note="3',5'-cAMP; via amide nitrogen"; /evidence="ECO:0000269|PubMed:21665969, ECO:0007744|PDB:2OZ6"; BINDING 185; /note="3',5'-cAMP"; /evidence="ECO:0000269|PubMed:21665969, ECO:0007744|PDB:2OZ6" |
| Calcium Binding |
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| catalytic Activity |
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| DNA Binding |
DNA_BIND 174..193; /note=H-T-H motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU00387 |
| EC Number |
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| Enzyme Function |
FUNCTION: Global cAMP-dependent transcriptional regulator that controls virulence gene expression by distinct cAMP-dependent and -independent mechanisms, which allow to fine tune its virulence program in response to specific host cues or environments (PubMed:20494996). Controls the expression of many regulatory targets including type II, type III and type IV secretion systems, flagellar-mediated motility, and quorum sensing systems (PubMed:9190808, PubMed:12057955, PubMed:26929300, PubMed:30761117). Transcriptional control is exerted by binding to a well-characterized consensus site (5'-ANWWTGNGAWNYAGWTCACAT) within target promoters (PubMed:17159200, PubMed:20494996, PubMed:26929300). Directly binds to the toxA upstream region to regulate exotoxin A production, to the lasR gene promoter to activate the las quorum-sensing system or to the exsA promoter to regulate type III secretion system (PubMed:9190808, PubMed:12057955, PubMed:19389782). Autoregulates as well its own expression (PubMed:20494996). {ECO:0000269|PubMed:12057955, ECO:0000269|PubMed:17159200, ECO:0000269|PubMed:19389782, ECO:0000269|PubMed:20494996, ECO:0000269|PubMed:26929300, ECO:0000269|PubMed:30761117, ECO:0000269|PubMed:9190808}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
NP_BIND 59..60; /note="3',5'-cAMP"; /evidence="ECO:0000269|PubMed:21665969, ECO:0007744|PDB:2OZ6"; NP_BIND 73..75; /note="3',5'-cAMP"; /evidence="ECO:0000269|PubMed:21665969, ECO:0007744|PDB:2OZ6"; NP_BIND 87..88; /note="3',5'-cAMP"; /evidence="ECO:0000269|PubMed:21665969, ECO:0007744|PDB:2OZ6"; NP_BIND 132..133; /note="3',5'-cAMP"; /evidence="ECO:0000269|PubMed:21665969, ECO:0007744|PDB:2OZ6" |
| Features |
Beta strand (11); Binding site (2); Chain (1); DNA binding (1); Domain (1); Helix (6); Nucleotide binding (4) |
| Keywords |
3D-structure;DNA-binding;Nucleotide-binding;Reference proteome;Transcription;Transcription regulation;Virulence;cAMP;cAMP-binding |
| Interact With |
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| Induction |
INDUCTION: Regulated by both cAMP and cGMP to allow differential regulation of different regulons (PubMed:12057955). Cyclic AMP is required for Vfr binding to vfr, regA, ptxR, and cpdA promoter DNA (PubMed:20494996, PubMed:25897033). Cyclic GMP instead inhibits the formation of Vfr-DNA complexes (PubMed:20494996, PubMed:25897033). {ECO:0000269|PubMed:12057955, ECO:0000269|PubMed:20494996, ECO:0000269|PubMed:25897033}. |
| Subcellular Location |
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| Modified Residue |
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| Post Translational Modification |
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| Signal Peptide |
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| Structure 3D |
X-ray crystallography (1) |
| Cross Reference PDB |
2OZ6;
|
| Mapped Pubmed ID |
- |
| Motif |
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| Gene Encoded By |
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| Mass |
24,225 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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