| IED ID | IndEnz0002018978 |
| Enzyme Type ID | protease018978 |
| Protein Name |
Carboxypeptidase Rv3627c EC 3.4.16.- |
| Gene Name | Rv3627c |
| 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 | MGPTRWRKSTHVVVGAAVLAFVAVVVAAAALVTTGGHRAGVRAPAPPPRPPTVKAGVVPVADTAATPSAAGVTAALAVVAADPDLGKLAGRITDALTGQELWQRLDDVPLVPASTNKILTAAAALLTLDRQARISTRVVAGGQNPQGPVVLVGAGDPTLSAAPPGQDTWYHGAARIGDLVEQIRRSGVTPTAVQVDASAFSGPTMAPGWDPADIDNGDIAPIEAAMIDAGRIQPTTVNSRRSRTPALDAGRELAKALGLDPAAVTIASAPAGARQLAVVQSAPLIQRLSQMMNASDNVMAECIGREVAVAINRPQSFSGAVDAVTSRLNTAHIDTAGAALVDSSGLSLDNRLTARTLDATMQAAAGPDQPALRPLLDLLPIAGGSGTLGERFLDAATDQGPAGWLRAKTGSLTAINSLVGVLTDRSGRVLTFAFISNEAGPNGRNAMDALATKLWFCGCTT |
| Enzyme Length | 461 |
| Uniprot Accession Number | O06380 |
| Absorption | |
| Active Site | ACT_SITE 114; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:P39844; ACT_SITE 117; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P39844; ACT_SITE 295; /evidence=ECO:0000250|UniProtKB:P39844 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.16.- |
| Enzyme Function | FUNCTION: Carboxypeptidase that cleaves terminal D-alanine from peptidoglycan in the mycobacterial cell wall. May cleave L-Lys-D-Ala and/or D-Ala-D-Ala peptide bonds. Exerts important effects on mycobacterial cell morphology and cell division. {ECO:0000269|PubMed:31000162}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Signal peptide (1) |
| Keywords | Carboxypeptidase;Cell wall biogenesis/degradation;Hydrolase;Protease;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,834 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |