| IED ID | IndEnz0002005057 |
| Enzyme Type ID | protease005057 |
| Protein Name |
Probable cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA CTL0301 |
| Organism | Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) |
| Taxonomic Lineage | cellular organisms Bacteria PVC group Chlamydiae Chlamydiia Chlamydiales Chlamydiaceae Chlamydia/Chlamydophila group Chlamydia Chlamydia trachomatis Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) |
| Enzyme Sequence | MVLLYSQASWDQRSKADALVLPFWMKNSKAQEAAVVDEDYKLVYQNALSNFSGKKGETAFLFGNDHTKEQKIVLLGLGKSEEVSGTTVLEAYAQATTVLRKAKCKTVNILFPTISQLRFSVEEFLTNLAAGVLSLNYNYPTYHKVDTSLPFLEKVTVMGIVSKVGDKIFRKEESLFEGVYLTRDLVNTNADEVTPEKLAAVAKGLAGEFASLDVKILDRKAILKEKMGLLAAVAKGAAVEPRFIVLDYQGKPKSKDRTVLIGKGVTFDSGGLDLKPGKAMITMKEDMAGAATVLGIFSALASLELPINVTGIIPATENAIGSAAYKMGDVYVGMTGLSVEIGSTDAEGRLILADAISYALKYCNPTRIIDFATLTGAMVVSLGESVAGFFANNDVLARDLAEASSETGEALWRMPLVEKYDQALHSDIADMKNIGSNRAGSITAALFLQRFLEDNPVAWAHLDIAGTAYHEKEELPYPKYATGFGVRCLIHYMEKFLSK |
| Enzyme Length | 499 |
| Uniprot Accession Number | B0B9F3 |
| Absorption | |
| Active Site | ACT_SITE 275; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 349; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| 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:0000255|HAMAP-Rule:MF_00181}; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; |
| DNA Binding | |
| EC Number | 3.4.11.1; 3.4.11.10 |
| Enzyme Function | FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. {ECO:0000255|HAMAP-Rule:MF_00181}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (7) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 54,185 |
| Kinetics | |
| Metal Binding | METAL 263; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 268; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 268; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 286; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 345; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 347; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 347; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Rhea ID | |
| Cross Reference Brenda |