IED ID | IndEnz0002005712 |
Enzyme Type ID | protease005712 |
Protein Name |
Probable exosortase EpsH EC 3.4.22.- |
Gene Name | epsH |
Organism | Methylobacillus sp. (strain 12S) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Nitrosomonadales Methylophilaceae Methylobacillus unclassified Methylobacillus Methylobacillus sp. (strain 12S) |
Enzyme Sequence | MEKHIKHAIRWPSLDTIPWAWVAIAIGLLILYFPTFWDLFHGLWGTERHAHGPIVFFVSIWFFYFKFKQLPEYGITYDPSPKLGWPILVLGLLLFILGRSQTLLIFEVGSLIPVLLGITLIFMGTRVAKFLWFAFFFLCFVVPLPAFVVDAATLPMKTAVSFATAHILYALDYPIARTGVMLTIGQYQLLVADACAGLNSLFTLEVLGLLYMNVTHHESPFRNFMLAVLIIPISFIANVTRVIVLALITYHWGDAAGQGFLHEFSGIVLFITALMLVIATDSLLRFFSRKFEKVPSTQSVDLKR |
Enzyme Length | 304 |
Uniprot Accession Number | Q83VR1 |
Absorption | |
Active Site | ACT_SITE 195; /note=Acyl-thioester intermediate; /evidence=ECO:0000250|UniProtKB:D4GUZ4; ACT_SITE 241; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:D4GUZ4 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the exosortase and its substrate, which is then transferred and covalently attached to the cell membrane (By similarity). This sortase may recognize a tripartite structure consisting of a conserved Pro-Glu-Pro (PEP) motif, followed by a transmembrane alpha helix domain and a cluster of basic residues, usually at the C-terminus of target proteins (Probable). {ECO:0000250|UniProtKB:D4GUZ4, ECO:0000305|PubMed:16930487}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Transmembrane (8) |
Keywords | Cell membrane;Hydrolase;Membrane;Protease;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 34,406 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |