Detail Information for IndEnz0002005712
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