| IED ID | IndEnz0010000487 |
| Enzyme Type ID | esterase000487 |
| Protein Name |
Putative peptidoglycan hydrolase Rv2525c EC 3.2.1.17 |
| Gene Name | Rv2525c LH57_13835 |
| Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| 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 ATCC 25618 / H37Rv) |
| Enzyme Sequence | MSVSRRDVLKFAAATPGVLGLGVVASSLRAAPASAGSLGTLLDYAAGVIPASQIRAAGAVGAIRYVSDRRPGGAWMLGKPIQLSEARDLSGNGLKIVSCYQYGKGSTADWLGGASAGVQHARRGSELHAAAGGPTSAPIYASIDDNPSYEQYKNQIVPYLRSWESVIGHQRTGVYANSKTIDWAVNDGLGSYFWQHNWGSPKGYTHPAAHLHQVEIDKRKVGGVGVDVNQILKPQFGQWA |
| Enzyme Length | 240 |
| Uniprot Accession Number | I6XEI5 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; Evidence={ECO:0000305|PubMed:25260828}; |
| DNA Binding | |
| EC Number | 3.2.1.17 |
| Enzyme Function | FUNCTION: May function as a peptidoglycan hydrolase with glycosidase activity (PubMed:25260828). In vitro, displays esterase activity toward p-nitrophenyl esters of various acyl chain length (C4 to C16), with a preference for p-nitrophenyl butyrate (C4) (PubMed:25869294). {ECO:0000269|PubMed:25869294, ECO:0000305|PubMed:25260828}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 38 degrees Celsius for the hydrolysis of p-nitrophenyl butyrate. {ECO:0000269|PubMed:25869294}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for the hydrolysis of p-nitrophenyl butyrate. {ECO:0000269|PubMed:25869294}; |
| Pathway | PATHWAY: Cell wall degradation; peptidoglycan degradation. {ECO:0000305|PubMed:25260828}. |
| nucleotide Binding | |
| Features | Chain (1); Mutagenesis (3); Signal peptide (1) |
| Keywords | 3D-structure;Cell wall biogenesis/degradation;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Upon exposure to antituberculous drugs such as isoniazid, ethionamide or PA-824, Rv2525c expression is significantly up-regulated together with those of other genes involved in cell wall processes. {ECO:0000269|PubMed:16952959}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16952959}. |
| Modified Residue | |
| Post Translational Modification | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000305|PubMed:16952959}. |
| Signal Peptide | SIGNAL 1..33; /note=Tat-type signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00648 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 4PMN; 4PMO; 4PMQ; 4PMR; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 25,370 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |