| IED ID | IndEnz0005000041 |
| Enzyme Type ID | lipase000041 |
| Protein Name |
PE cleavage protein A PE-PGRS family protein PE_PGRS35 |
| Gene Name | pecA PE_PGRS35 MT2036 |
| Organism | Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) |
| Enzyme Sequence | MSFLVVVPEFLTSAAADVENIGSTLRAANAAAAASTTALAAAGADEVSAAVAALFARFGQEYQAVSAQASAFHQQFVQTLNSASGSYAAAEATIASQLQTAQHDLLGAVNAPTETLLGRPLIGDGAPGTATSPNGGAGGLLYGNGGNGYSATASGVGGGAGGSAGLIGNGGAGGAGGPNAPGGAGGNGGWLLGNGGIGGPGGASSIPGMSGGAGGTGGAAGLLGWGANGGAGGLGDGVGVDRGTGGAGGRGGLLYGGYGVSGPGGDGRTVPLEIIHVTEPTVHANVNGGPTSTILVDTGSAGLVVSPEDVGGILGVLHMGLPTGLSISGYSGGLYYIFATYTTTVDFGNGIVTAPTAVNVVLLSIPTSPFAISTYFSALLADPTTTPFEAYFGAVGVDGVLGVGPNAVGPGPSIPTMALPGDLNQGVLIDAPAGELVFGPNPLPAPNVEVVGSPITTLYVKIDGGTPIPVPSIIDSGGVTGTIPSYVIGSGTLPANTNIEVYTSPGGDRLYAFNTNDYRPTVISSGLMNTGFLPFRFQPVYIDYSPSGIGTTVFDHPA |
| Enzyme Length | 558 |
| Uniprot Accession Number | P9WIF0 |
| Absorption | |
| Active Site | ACT_SITE 297; /evidence=ECO:0000250|UniProtKB:B2HE92 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Aspartic protease that processes the lipase LipY and other PE_PGRS proteins. Can also cleave itself. {ECO:0000250|UniProtKB:B2HE92}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1) |
| Keywords | Aspartyl protease;Hydrolase;Protease;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:B2HE92}. Cell surface {ECO:0000250|UniProtKB:B2HE92}. Note=Secreted via the ESX-5 / type VII secretion system (T7SS). {ECO:0000250|UniProtKB:B2HE92}. |
| Modified Residue | |
| Post Translational Modification | PTM: Undergoes auto-proteolytic processing. {ECO:0000250|UniProtKB:B2HE92}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,738 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |