PPIRE13303

Target Protein Information
Protein_Name Periplasmic pH-dependent serine endoprotease DegQ
Protein_Sequence MKKQTQLLSALALSVGLTLSASFQAVASIPGQVADQAPLPSLAPMLEKVLPAVVSVRVEGTASQGQKIPEEFKKFFGDDLPDQPAQPFEGLGSGVIINASKGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIVSALGRSGLNLEGLENFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFAIPSNMARTLAQQLIDFGEIKRGLLGIKGTEMSADIAKAFNLDVQRGAFVSEVLPGSGSAKAGVKAGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGKPLEVEVTLDTSTSSSASAEMITPALEGATLSDGQLKDGGKGIKIDEVVKGSPAAQAGLQKDDVIIGVNRDRVNSIAEMRKVLAAKPAIIALQIVRGNESIYLLMR
Organism_Source Escherichia coli (strain K12)
Functional_Classification serine proteases
Cellular_Localization Extracellular
Gene_Names degQ
UniProt_ID P39099
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name DegQ activating peptide
Peptide_Sequence SPMFKGVLDMMYGGMRGYQV
Peptide_Length 20
Peptide_SMILES CSCC[C@H](NC(=O)CNC(=O)CNC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCSC)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCSC)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](N)CO)C(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)NCC(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)O)C(C)C
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 2267.72
Aliphatic_Index 48.50000
Aromaticity 0.15000
Average_Rotatable_Bonds 3.70000
Charge_at_pH_7 0.99643
Isoelectric_Point 9.14509
Number_of_Hydrogen_Bond_Acceptors 32
Number_of_Hydrogen_Bond_Donors 29
Topological_Polar_Surface_Area 836.43000
X_logP_energy -5.72413
Interaction Information
Affinity KD=16 uM
Affinity_Assay Isothermal titration calorimetry
PDB_ID 3STJ
Type Allosteric modulator
Structure
Reference Information
Document_Type Research Articles
Title Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.
Release_Year 2011
PMID 21685389
DOI 10.1074/jbc.M111.243832