Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.
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DegP combines molecular chaperone and protease functions, with chaperone activity favored at low temperature and proteolysis at elevated temperature.
"The chaperone function dominates at low temperatures, while the proteolytic activity is present at elevated temperatures."
PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease.
The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress.
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HtrA/DegP protects against envelope-associated oxidative damage and localizes to the periplasmic face of the inner membrane.
"HtrA plays a role in defense against oxidative shock and support the hypothesis that HtrA participates in the degradation of oxidatively damaged proteins localized in the cell envelope"
Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine.
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The DegP resting structure is a hexamer of trimeric rings with internally sequestered protease active sites and PDZ-domain sidewalls.
"The DegP hexamer is formed by staggered association of trimeric rings."
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
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SurA is the major OMP transit chaperone; Skp and DegP have a rescue role when OMPs fall off the SurA pathway.
"Evidence presented suggests that DegP/Skp function to rescue OMPs that fall off the SurA pathway."
Structural basis for the regulated protease and chaperone function of DegP.
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Misfolded protein binding converts DegP hexamers into active 12- and 24-mers; folded OMP protomer encapsulation may support safe transit whereas misfolded substrates are eliminated.
"binding of misfolded proteins transforms hexameric DegP into large, catalytically active 12-meric and 24-meric multimers."
Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins.
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DegP PDZ1 captures misfolded substrates and activates processive serine endoproteolysis into oligopeptides.
"PDZ1 functions as the primary substrate binding site that captures the C-terminal Z-motif of misfolded proteins and reaction intermediates and presents the N-terminal segment to the protease domain."
Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins.
Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control.
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DegP can form membrane-associated bowl-like oligomers with enhanced protease and reduced chaperone activity.
"they exhibit higher proteolytic and lower chaperone-like activities than DegP in solution."
HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues.
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Peptide binding to DegP PDZ domains triggers conversion from resting DegP6 to proteolytically active DegP12/DegP24.
"effector-peptide binding to the PDZ domain of DegP induces oligomer conversion from resting hexameric DegP6 into proteolytically active 12-mers and 24-mers"
Determinants of structural and functional plasticity of a widely conserved protease chaperone complex.
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Mutational and refolding experiments identify how PDZ1 peptide binding is transmitted allosterically to the protease-domain substrate pocket.
"Binding of specific peptides to PDZ domain-1 causes a local rearrangement that is allosterically transmitted to the substrate-binding pocket of the protease domain."
Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages.
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Linked active-site and PDZ1 degrons in substrates drive cooperative assembly of active DegP cages that remain assembled until substrate is depleted.
"active cages assemble rapidly in a reaction that is positively cooperative in substrate concentration, remain stably assembled while uncleaved substrate is present, and dissociate once degradation is complete."
The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase.
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Purified DegP/HtrA is a DFP-sensitive serine endopeptidase processed from a precursor.
"The HtrA protein was shown to be a specific endopeptidase which was inhibited by diisopropylfluorophosphate, suggesting that HtrA is a serine protease."
Characterization of the structure and function of Escherichia coli DegQ as a representative of the DegQ-like proteases of bacterial HtrA family proteins.
DegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in the Gram-negative bacterium Escherichia coli.
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OMPs are major natural DegP substrates, and DegP's dominant in vivo role is proteolytic clearance of unfolded OMPs.
"We also demonstrated that DegP primarily functions as a protease, at both low and high temperatures, to eliminate unfolded OMPs"
Substrate occupancy at the onset of oligomeric transitions of DegP.
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Native mass spectrometry showed that substrate-mimicking peptide ligands bind the resting 6-mer before active-state transition.
"binding of multiple substrate-mimicking peptide ligands to the DegP resting state occurs prior to the transition to an active conformation."
Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures.
Detecting envelope stress by monitoring β-barrel assembly.
The role of the LB structural loop and its interactions with the PDZ domain of the human HtrA3 protease.
An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins.
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degP mutants fail to degrade an abnormal membrane-bound alkaline phosphatase fusion and several abnormal periplasmic proteins.
"One mutant is also defective in breakdown of five other abnormal periplasmic proteins but not of two cytoplasmic proteins."
Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures.
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Ser210 and His105 active-site substitutions eliminate DegP protease activity and complementation of htrA thermosensitivity.
"Mutational alteration of Ser210 eliminated proteolytic activity of HtrA. An identical effect was observed when His105 was mutated."
Evidence for PDZ domains in bacteria, yeast, and plants.
HtrA heat shock protease interacts with phospholipid membranes and undergoes conformational changes.
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HtrA/DegP associates peripherally with the inner membrane and its activity is affected by phospholipids.
"HtrA is a peripheral membrane protein, localized on the periplasmic side of the inner membrane."