| IED ID | IndEnz0002010919 |
| Enzyme Type ID | protease010919 |
| Protein Name |
Peptidoglycan endopeptidase RipA EC 3.4.-.- Macrophage invasion and intracellular persistence protein A Resuscitation-promoting factor interaction partner A Rpf-interacting protein A |
| Gene Name | ripA Rv1477 |
| 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 | MRRNRRGSPARPAARFVRPAIPSALSVALLVCTPGLATADPQTDTIAALIADVAKANQRLQDLSDEVQAEQESVNKAMVDVETARDNAAAAEDDLEVSQRAVKDANAAIAAAQHRFDTFAAATYMNGPSVSYLSASSPDEIIATVTAAKTLSASSQAVMANLQRARTERVNTESAARLAKQKADKAAADAKASQDAAVAALTETRRKFDEQREEVQRLAAERDAAQARLQAARLVAWSSEGGQGAPPFRMWDPGSGPAGGRAWDGLWDPTLPMIPSANIPGDPIAVVNQVLGISATSAQVTANMGRKFLEQLGILQPTDTGITNAPAGSAQGRIPRVYGRQASEYVIRRGMSQIGVPYSWGGGNAAGPSKGIDSGAGTVGFDCSGLVLYSFAGVGIKLPHYSGSQYNLGRKIPSSQMRRGDVIFYGPNGSQHVTIYLGNGQMLEAPDVGLKVRVAPVRTAGMTPYVVRYIEY |
| Enzyme Length | 472 |
| Uniprot Accession Number | O53168 |
| Absorption | |
| Active Site | ACT_SITE 383; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"; ACT_SITE 432; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"; ACT_SITE 444; /evidence="ECO:0000255|PROSITE-ProRule:PRU01284, ECO:0000305|PubMed:20826344" |
| Activity Regulation | ACTIVITY REGULATION: The synergistic effects on peptidoglycan degradation of RipA plus RpfB are inhibited by addition of PBP1A (ponA1). {ECO:0000269|PubMed:20686708}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages. {ECO:0000269|PubMed:16495549, ECO:0000269|PubMed:17919286, ECO:0000269|PubMed:18463693, ECO:0000269|PubMed:20826344, ECO:0000269|PubMed:21864539}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 5 and 5.5.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (9); Chain (1); Domain (1); Helix (10); Mutagenesis (3); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Cell wall biogenesis/degradation;Hydrolase;Protease;Reference proteome;Secreted;Signal;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17919286}. Note=Localizes to the septa upon expression in M.bovis or M.smegmatis. Remains associated with the cell. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..39; /evidence=ECO:0000305 |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 2XIV; 3NE0; 3PBC; 3S0Q; 4Q4G; 4Q4N; 4Q4T; 6EWY; |
| Mapped Pubmed ID | 25195744; 29722065; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,808 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |