| IED ID | IndEnz0002004230 |
| Enzyme Type ID | protease004230 |
| Protein Name |
Serine protease Hip1 EC 3.4.21.- Carboxylesterase A |
| Gene Name | hip1 caeA MT2282 |
| 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 | MGMRLSRRDKIARMLLIWAALAAVALVLVGCIRVVGGRARMAEPKLGQPVEWTPCRSSNPQVKIPGGALCGKLAVPVDYDRPDGDVAALALIRFPATGDKIGSLVINPGGPGESGIEAALGVFQTLPKRVHERFDLVGFDPRGVASSRPAIWCNSDADNDRLRAEPQVDYSREGVAHIENETKQFVGRCVDKMGKNFLAHVGTVNVAKDLDAIRAALGDDKLTYLGYSYGTRIGSAYAEEFPQRVRAMILDGAVDPNADPIEAELRQAKGFQDAFNNYAADCAKNAGCPLGADPAKAVEVYHSLVDPLVDPDNPRISRPARTKDPRGLSYSDAIVGTIMALYSPNLWQHLTDGLSELVDNRGDTLLALADMYMRRDSHGRYNNSGDARVAINCVDQPPVTDRDKVIDEDRRAREIAPFMSYGKFTGDAPLGTCAFWPVPPTSQPHAVSAPGLVPTVVVSTTHDPATPYKAGVDLANQLRGSLLTFDGTQHTVVFQGDSCIDEYVTAYLIGGTTPPSGAKC |
| Enzyme Length | 520 |
| Uniprot Accession Number | P9WHR2 |
| Absorption | |
| Active Site | ACT_SITE 228; /note=Nucleophile; /evidence=ECO:0000305|PubMed:17428787; ACT_SITE 463; /evidence=ECO:0000305|PubMed:17428787; ACT_SITE 490; /note=Proton donor; /evidence=ECO:0000305|PubMed:17428787 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease that promotes tuberculosis (TB) pathogenesis by promoting the processing and the extracellular release of the M.tuberculosis (Mtb) heat-shock protein GroEL2 (By similarity). In vitro, catalyzes the cleavage of ester bonds. Esterase activity increases with increasing carbon chain length of the substrate (PubMed:17428787). {ECO:0000250|UniProtKB:P9WHR3, ECO:0000269|PubMed:17428787}.; FUNCTION: Key immunomodulatory virulence factor, which promotes survival in host macrophages and modulates host immune responses. {ECO:0000250|UniProtKB:P9WHR3}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:17428787}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Erroneous initiation (1); Lipidation (2); Mutagenesis (3); Signal peptide (1) |
| Keywords | Cell membrane;Hydrolase;Lipoprotein;Membrane;Palmitate;Signal;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell envelope {ECO:0000269|PubMed:17428787}. Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255|PROSITE-ProRule:PRU00303 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,924 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=738 uM for 4-methylumbelliferyl butyrate {ECO:0000269|PubMed:17428787}; Vmax=128 umol/min/mg enzyme with 4-methylumbelliferyl butyrate as substrate {ECO:0000269|PubMed:17428787}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |