IED ID | IndEnz0005000032 |
Enzyme Type ID | lipase000032 |
Protein Name |
Esterase PE11 EC 3.1.1.6 PE family protein PE11 |
Gene Name | PE11 lipX Rv1169c |
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 | MSFVTTRPDSIGETAANLHEIGVTMSAHDDGVTPLITNVESPAHDLVSIVTSMLFSMHGELYKAIARQAHVIHESFVQTLQTSKTSYWLTELANRAGTST |
Enzyme Length | 100 |
Uniprot Accession Number | Q79FR5 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; EC=3.1.1.6; Evidence={ECO:0000269|PubMed:26902658}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:26902658}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:26902658}; |
DNA Binding | |
EC Number | 3.1.1.6 |
Enzyme Function | FUNCTION: Involved in cell wall lipids remodeling and in virulence (PubMed:26157429, PubMed:26902658, PubMed:28198348). Restricts the biofilm growth and is essential for the optimal intracellular survival of M.tuberculosis (PubMed:28198348). Shows esterase activity with a preference for short-chain esters, particularly pNP-acetate (C2) and pNP-butyrate (C4) (PubMed:26902658). Has weaker activity with pNP-octanoate (C8), pNP-laurate (C12) and pNP-myristate (C14) (PubMed:26902658). Shows weak long-chain triacylglycerol (TAG) hydrolase activity in vitro (PubMed:16354661). Not necessary for PPE17 stability or for its localization on the mycobacterial surface (PubMed:23469198). {ECO:0000269|PubMed:16354661, ECO:0000269|PubMed:23469198, ECO:0000269|PubMed:26157429, ECO:0000269|PubMed:26902658, ECO:0000269|PubMed:28198348}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Domain (1) |
Keywords | Cell wall;Cell wall biogenesis/degradation;Hydrolase;Reference proteome;Secreted;Virulence |
Interact With | |
Induction | INDUCTION: Coexpressed with PPE17. {ECO:0000269|PubMed:23469198, ECO:0000269|PubMed:28198348}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:26157429}. Note=Cell wall associated protein. {ECO:0000269|PubMed:26157429}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 10,872 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:12957; RHEA:47348; RHEA:47356 |
Cross Reference Brenda |