| IED ID | IndEnz0002010588 |
| Enzyme Type ID | protease010588 |
| Protein Name |
Metalloprotease PmbA EC 3.4.-.- Protein TldE |
| Gene Name | pmbA tldE b4235 JW4194 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MALAMKVISQVEAQRKILEEAVSTALELASGKSDGAEVAVSKTTGISVSTRYGEVENVEFNSDGALGITVYHQNRKGSASSTDLSPQAIARTVQAALDIARYTSPDPCAGVADKELLAFDAPDLDLFHPAEVSPDEAIELAARAEQAALQADKRITNTEGGSFNSHYGVKVFGNSHGMLQGYCSTRHSLSSCVIAEENGDMERDYAYTIGRAMSDLQTPEWVGADCARRTLSRLSPRKLSTMKAPVIFANEVATGLFGHLVGAIAGGSVYRKSTFLLDSLGKQILPDWLTIEEHPHLLKGLASTPFDSEGVRTERRDIIKDGILTQWLLTSYSARKLGLKSTGHAGGIHNWRIAGQGLSFEQMLKEMGTGLVVTELMGQGVSAITGDYSRGAAGFWVENGEIQYPVSEITIAGNLKDMWRNIVTVGNDIETRSNIQCGSVLLPEMKIAGQ |
| Enzyme Length | 450 |
| Uniprot Accession Number | P0AFK0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA). {ECO:0000269|PubMed:12029038}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (14); Chain (1); Helix (11); Turn (2) |
| Keywords | 3D-structure;Cytoplasm;Hydrolase;Metalloprotease;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 5NJ5; 5NJ9; 5NJA; 5NJB; 5NJC; 5NJF; |
| Mapped Pubmed ID | 16606699; 28943336; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,370 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |