IED ID | IndEnz0002010226 |
Enzyme Type ID | protease010226 |
Protein Name |
Cysteine protease StiP EC 3.4.22.- |
Gene Name | stiP ACIAD1960 |
Organism | Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Moraxellales Moraxellaceae Acinetobacter Acinetobacter baylyi Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) |
Enzyme Sequence | MAIINKDKATELILKQGFSGSYQSEQVTFLLKRTHIEPTDTAEKERLIQSGEKHYSQMISLENAPTARHLELFEQAMQQGQQRLAQEVQQLAQTLVVEFNEPIVLVSFVRAGVPLGVLLYHAIQDLGRDCVHYGISIIRDRGIDFAALETIIARHGHASIVFVDGWTGKGAIRQELQRSLGNDTRFIGKPLPLVVLSDIAGCAWLAASGDDWLIPSGILGSTISGLISRSICEGETLSADEITAENIDQWHRCIEYHHLKEFDISQQFIQRINQIRLKLNPQSNAVWAETQQQAQQDQSQQVVHKLAQEYDIQNINRIKPSIAEATRAILRRVPDLVLLRDADDEDTRLLRHLTQITKTPVQVVGDQIAPYRAITLIQKLGKG |
Enzyme Length | 383 |
Uniprot Accession Number | Q6FAX7 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Is inhibited by bromopyruvate in vitro. Activity is not affected by the presence of tellurite. {ECO:0000269|PubMed:24206355}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Cysteine protease that may play a role in regulating cell morphology in response to stressful conditions which likely cause oxidative damage. Appears to catalyze its own cleavage, which probably leads to its activation. {ECO:0000269|PubMed:24206355}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Propeptide (1) |
Keywords | Autocatalytic cleavage;Hydrolase;Protease;Reference proteome;Thiol protease |
Interact With | |
Induction | INDUCTION: Highly induced by starvation during long-term stationary phase, while shows very low expression during exponential growth. {ECO:0000269|PubMed:20511417}. |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | PTM: Is probably processed via an autocatalytic removal of a proregion of about 100 amino acids. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 42,995 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |