| IED ID | IndEnz0002010464 |
| Enzyme Type ID | protease010464 |
| Protein Name |
Probable lipoprotein aminopeptidase LpqL EC 3.4.11.1 Leucine aminopeptidase Lipoprotein LpqL |
| Gene Name | lpqL Rv0418 LH57_02235 |
| 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 | MVNKSRMMPAVLAVAVVVAFLTTGCIRWSTQSRPVVNGPAAAEFAVALRNRVSTDAMMAHLSKLQDIANANDGTRAVGTPGYQASVDYVVNTLRNSGFDVQTPEFSARVFKAEKGVVTLGGNTVEARALEYSLGTPPDGVTGPLVAAPADDSPGCSPSDYDRLPVSGAVVLVDRGVCPFAQKEDAAAQRGAVALIIADNIDEQAMGGTLGANTDVKIPVVSVTKSVGFQLRGQSGPTTVKLTASTQSFKARNVIAQTKTGSSANVVMAGAHLDSVPEGPGINDNGSGVAAVLETAVQLGNSPHVSNAVRFAFWGAEEFGLIGSRNYVESLDIDALKGIALYLNFDMLASPNPGYFTYDGDQSLPLDARGQPVVPEGSAGIERTFVAYLKMAGKTAQDTSFDGRSDYDGFTLAGIPSGGLFSGAEVKKSAEQAELWGGTADEPFDPNYHQKTDTLDHIDRTALGINGAGVAYAVGLYAQDLGGPNGVPVMADRTRHLIAKP |
| Enzyme Length | 500 |
| Uniprot Accession Number | P96264 |
| Absorption | |
| Active Site | ACT_SITE 316; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P80561 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000250|UniProtKB:Q9HZQ8}; |
| DNA Binding | |
| EC Number | 3.4.11.1 |
| Enzyme Function | FUNCTION: An aminopeptidase; acts on free N-terminal amino groups with a very strong preference for Leu in the first position. {ECO:0000250|UniProtKB:Q9HZQ8}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Lipidation (2); Metal binding (6); Signal peptide (1); Site (1) |
| Keywords | Aminopeptidase;Cell membrane;Hydrolase;Lipoprotein;Membrane;Metal-binding;Palmitate;Protease;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:24093492}. |
| Modified Residue | |
| Post Translational Modification | PTM: Modified by Lgt on Cys-25 with an S-linked diacylglycerol with a mixture of C16 and C19 fatty acids (palmitic and tuberculostearic acid), signal peptide is removed by LspA, modified by Lnt with an amide-linked mixture of C16 and C19 fatty acids, expressed in M.bovis (PubMed:24093492). {ECO:0000269|PubMed:24093492}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255|PROSITE-ProRule:PRU00303 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,042 |
| Kinetics | |
| Metal Binding | METAL 271; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 283; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 283; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 317; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 345; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 448; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561 |
| Rhea ID | |
| Cross Reference Brenda |