Detail Information for IndEnz0002010688
IED ID IndEnz0002010688
Enzyme Type ID protease010688
Protein Name Tripeptidyl aminopeptidase
Tap
EC 3.4.14.-
Gene Name tap
Organism Streptomyces lividans
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces lividans
Enzyme Sequence MRKSSIRRRATAFGTAGALVTATLIAGAVSAPAASAAPADGHGHGRSWDREARGAAIAAARAARAGIDWEDCAADWNLPKPIQCGYVTVPMDYAKPYGKQIRLAVDRIGNTGTRSERQGALIYNPGGPGGSGLRFPARVTNKSAVWANTAKAYDFVGFDPRGVGHSAPISCVDPQEFVKAPKADPVPGSEADKRAQRKLAREYAEGCFERSGEMLPHMTTPNTARDLDVIRAALGEKKLNYLGVSYGTYLGAVYGTLFPDHVRRMVVDSVVNPSRDKIWYQANLDQDVAFEGRWKDWQDWVAANDAAYHLGDTRAEVQDQWLKLRAAAAKKPLGGVVGPAELISFFQSAPYYDSAWAPTAEIFSKYVAGDTQALVDAAAPDLSDTAGNASAENGNAVYTAVECTDAKWPANWRTWDRDNTRLHRDHPFMTWANAWMNLPCATWPVKQQTPLNVKTGKGLPPVLIVQSERDAATPYEGAVELHQRFRGSRLITERDAGSHGVTGLVNPCINDRVDTYLLTGRTDARDVTCAPHATPRP
Enzyme Length 537
Uniprot Accession Number Q54410
Absorption
Active Site ACT_SITE 245; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 470; /evidence=ECO:0000250; ACT_SITE 499; /note=Proton donor; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.14.-
Enzyme Function FUNCTION: Cleaves tripeptides from the N-termini of proteins. Does not cleave mono- or dipeptides, or N-terminally blocked peptides. {ECO:0000269|PubMed:7487044}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (1); Propeptide (1); Signal peptide (1)
Keywords Aminopeptidase;Direct protein sequencing;Hydrolase;Protease;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7487044}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..36; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 58,273
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda