Detail Information for IndEnz0002014311
IED ID IndEnz0002014311
Enzyme Type ID protease014311
Protein Name Probable periplasmic serine endoprotease DegP-like
EC 3.4.21.107
Protease Do
Gene Name Psefu_3239
Organism Pseudomonas fulva (strain 12-X)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas putida group Pseudomonas fulva Pseudomonas fulva (strain 12-X)
Enzyme Sequence MSMPSLKKYAAALFAVFLMGQSVAAHAQLPDFTPLVEAASPAVVNISTRQKVPNAVASNGGLSVPDLEGLPPMFREFFERSIPQQPRAPGGGGRQREAQSLGSGFIISKDGYILTNNHVVADADEIIVRLSDRSELEAKLIGTDPRSDVALLKVEANDLPTVKLGNSDNLKVGEWVLAIGSPFGFDHSVTAGIVSAKGRSLPNESYVPFIQTDVAINPGNSGGPLFNLDGEVVGINSQIFTRSGGFMGLSFAIPMSVAMDVADQLKASGKVSRGWLGVVIQEVNKDLAESFGLEKPAGALVAQVLEDGPAAKGGLQVGDVILSLDGKPIIMSADLPHLVGALKPGTKANLEIVREGSRKTLKVAVGTMPADDGDEATNDAAPSAERSSNRLGVSVAELTDEQKKALDLRGGVVIREVQDGPAALIGLRPGDVITHLNNQAITSAKNFTEVAQSLPKNRSVSMRVLRQGRASFITFKLAE
Enzyme Length 479
Uniprot Accession Number F6AA62
Absorption
Active Site ACT_SITE 118; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 148; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 221; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.; EC=3.4.21.107;
DNA Binding
EC Number 3.4.21.107
Enzyme Function FUNCTION: Might be efficient in the degradation of transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (2); Region (3); Signal peptide (1)
Keywords Hydrolase;Periplasm;Protease;Reference proteome;Repeat;Serine protease;Signal;Stress response
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..27; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 50,338
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda