Detail Information for IndEnz0002009188
IED ID IndEnz0002009188
Enzyme Type ID protease009188
Protein Name Protease inhibitor
BBRPI

Cleaved into: Serine protease inhibitor; Serine protease inhibitor C; Serine protease inhibitor B; Serine protease inhibitor A
Gene Name
Organism Brevibacillus choshinensis
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Brevibacillus Brevibacillus choshinensis
Enzyme Sequence MKTIRTGMMTLAALAVLGTNVVSATSEPVKELSVNVNGQHIEQAAIFDKGQQTVLVPLRDVAESLGFQVKWNAETKAAEVNKGAIFSYAKVGEDRYPFAKMYKTLGAEPRLLNGNTYVPVAFVDEILQAEVNVTDDAVTVVDEESDVAPVRTGTITTLNKREDGGVSFQLNGYETGIILHVDKETKITTADGKELKPEDLQLGMEVEATHQKFMAMSMPQSGAVSIVVKSGLETPEVLGTAGKVASIDKDQEGSYKMLVEGQALAENAPEKVALIVGKDTKIVSAKDNKELAPEDLKAEMKVFAYYGPKLTRSLPPIGVAEKIVVE
Enzyme Length 326
Uniprot Accession Number P43131
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Shows inhibitory activity towards serine proteases, such as trypsin, chymotrypsin and subtilisin. May form a trypsin-inhibitor complex in a molar ratio of 1:1.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable at neutral and acidic pHs.;
PH Dependency
Pathway
nucleotide Binding
Features Chain (4); Region (1); Repeat (2); Signal peptide (1)
Keywords Direct protein sequencing;Protease inhibitor;Repeat;Secreted;Serine protease inhibitor;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification PTM: Proteolytically cleaved to yield at least three forms (BBRPI-A, -B, and -C).
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000269|PubMed:1610177
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 35,100
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda