| IED ID | IndEnz0005001139 |
| Enzyme Type ID | lipase001139 |
| Protein Name |
SL1278 acyltransferase Chp1 EC 2.3.1.284 Cutinase-like hydrolase protein |
| Gene Name | chp1 Rv3822 RVBD_3822 LH57_20830 P425_03980 |
| 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 | MKCPGVSDCVATVRHDNVFAIAAGLRWSAAVPPLHKGDAVTKLLVGAIAGGMLACAAILGDGIASADTALIVPGTAPSPYGPLRSLYHFNPAMQPQIGANYYNPTATRHVVSYPGSFWPVTGLNSPTVGSSVSAGTNNLDAAIRSTDGPIFVAGLSQGTLVLDREQARLANDPTAPPPGQLTFIKAGDPNNLLWRAFRPGTHVPIIDYTVPAPAESQYDTINIVGQYDIFSDPPNRPGNLLADLNAIAAGGYYGHSATAFSDPARVAPRDITTTTNSLGATTTTYFIRTDQLPLVRALVDMAGLPPQAAGTVDAALRPIIDRAYQPGPAPAVNPRDLVQGIRGIPAIAPAIAIPIGSTTGASAATSTAAATAAATNALRGANVGPGANKALSMVRGLLPKGKKH |
| Enzyme Length | 404 |
| Uniprot Accession Number | O07801 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Activity is potentiated by the SL-1 transporter MmpL8. Inhibited by the lipase inhibitor tetrahydrolipstatin (THL). {ECO:0000269|PubMed:22194604}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=3 3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-alpha,alpha-trehalose = 3,6,6'-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2'-sulfo-alpha-alpha-trehalose + 2 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose.; EC=2.3.1.284; Evidence={ECO:0000269|PubMed:22194604}; |
| DNA Binding | |
| EC Number | 2.3.1.284 |
| Enzyme Function | FUNCTION: Involved in the final steps of the cell wall sulfolipid-1 (SL-1) biosynthesis. Catalyzes two successive acylations of the precursor 2-palmitoyl-3-(C43)-phthioceranyl-alpha, alpha'-D-trehalose-2'-sulfate (SL1278) to yield the tetraacylated sulfolipid SL-1. {ECO:0000269|PubMed:22194604}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Mutagenesis (1); Topological domain (2); Transmembrane (1) |
| Keywords | Acyltransferase;Cell inner membrane;Cell membrane;Lipid biosynthesis;Lipid metabolism;Membrane;Reference proteome;Transferase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:22194604}; Single-pass membrane protein {ECO:0000255}. Note=The catalytic site is on the cytoplasmic side of the inner membrane. {ECO:0000269|PubMed:22194604}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,408 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 2.3.1.284; |