Detail Information for IndEnz0002019242
IED ID IndEnz0002019242
Enzyme Type ID protease019242
Protein Name Ecotin
Gene Name eco eti b2209 JW2197
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MKTILPAVLFAAFATTSAWAAESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLENKTLEGWGYDYYVFDKVSSPVSTMMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTPDNVDVKYRVWKAEEKIDNAVVR
Enzyme Length 162
Uniprot Accession Number P23827
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (13); Chain (1); Disulfide bond (1); Erroneous initiation (1); Helix (3); Signal peptide (1); Site (1); Turn (1)
Keywords 3D-structure;Direct protein sequencing;Disulfide bond;Periplasm;Protease inhibitor;Reference proteome;Serine protease inhibitor;Signal
Interact With P03951; P00763
Induction
Subcellular Location SUBCELLULAR LOCATION: Periplasm.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..20; /evidence="ECO:0000269|PubMed:2007606, ECO:0000269|PubMed:9298646"
Structure 3D X-ray crystallography (20)
Cross Reference PDB 1AZZ; 1ECY; 1ECZ; 1EZS; 1EZU; 1FI8; 1ID5; 1IFG; 1N8O; 1P0S; 1SLU; 1SLV; 1SLW; 1SLX; 1XX9; 1XXD; 1XXF; 4IW4; 4NIY; 7CBK;
Mapped Pubmed ID 10966645; 10966646; 11352586; 12834348; 14579355; 1537814; 15545266; 16606699; 23861840; 24520050; 32657577; 8508953; 8634241; 9518472; 9521759;
Motif
Gene Encoded By
Mass 18,192
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda