| IED ID | IndEnz0002008235 |
| Enzyme Type ID | protease008235 |
| Protein Name |
Ubiquitinating enzyme SidE Includes: Deubiquitinase DUB EC 3.4.22.- Deubiquitinating enzyme ; Ubiquitin transferase EC 2.3.2.- ; Mono-ADP-ribosyltransferase mART EC 2.4.2.31 |
| Gene Name | sidE lpg0234 |
| Organism | Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Legionellales Legionellaceae Legionella Legionella pneumophila Legionella pneumophila subsp. pneumophila Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) |
| Enzyme Sequence | MPKYVEGIELTQEGMHAIFERMGHPNITSGTIYNGEPTIDKGALDRQGFMPVLTGVSPRQDSGHWIMLIKGQGNQYFLFDPLGESSGKYYQNILAKKLPGATLSVIPNNAGLNMGLCGYWVASVGLRAHAALTQPIPPSLRNLGQTITQEMRDELTQDGSEKITQWLRAVGNEFPDGDIQPDATALRRATEKNVRIDEFQPVLTGTSPKEISINPTAPQEVSVPTWNGFSLYTDETVRNAARYAYDNYLGKPYTGTVEATPVNFGGQMVYRQHHGLAHTLRTMAYAEIIVEEARKAKLRGESLKTFADGRTLADVTPEELRKIMIAQAFFVTGRDDEESSKNYEKYHEQSRDAFLKYVEENKSTLIPDVFKDEKDVKFYADVIEDKDHKWADSPAHVLVNQGHMVDLVRVKQPPESYLEYYFSQLQPWIGSTATEAVFATQRQFFHATYEAVAGFDSENKEPHLVVDGLGRYVIGQDGNPIREESDDEDEEESGELKFFSQKKKLEENQRYMRVDEYLKLDEVQKRFPGAGKKLDGGLPGLKEYQYLQRLNSINRARCENDVDFCLGQLQTAHHQTKITPIKRAFQSSSEKARRQPNMDEIAAARIVQQIMANPDCIHDDHVFLNGQKLEEKFFRDLLAKCDMAIVGSLLNDTDIRNIDTLMQHERNTEFHSTDAKAKPVKLGETWEKTIRSGGGVTQIKHDLIFLMQNDAWYHTRVNAIAQNRDKDSTFKEVLITALMTPLTNKSLMDTSRSPAPKTLFRGLDLSEEFKNKLINQAETIIANTTEHLFTDLSTEAFKQIKLNDFSQVSARTCASTSTNIEVPRTIFGSNTIFEILDPDGLLHPKQVGTHVSGSESEYSIYLPEDVALVPIKVSFDGKTGKGKDRHIFTLVAVKSPDFTPRHESGYAVGPLLKMQTPKLEEIQRLVEQAREEPDLERVFNLQSRVARQAKFSTESGYKTFLNEKVAPVLEQSLNGLLDNNVTILGKVLSAFPSDGQWSAFNSVEARQMKIQMDAIKQMVEKKAVLEGQILPALAQCQNALEKQNIAGALQALRNIPSEKEMQTMLSISGGLRGQIQRAKQDLTETLEPLQRAITAKLVSDQEKVKVRYEKLIAGIPQQIADLEKAELADLAKVKKVVSRFNHLQEELKLLRNEKIRMHTGSEKVDFSDIAQLEAQLQKIHTKLYDAYLVELTKEISALVKEKPKNLADVKRMVSNFYAMSADIEQLRQEKIKEHGESKDPIDMSDIDKLKEELQKINQFLVKAMGTNIRVSLNQMEVKTFDAQEKEAQQNLKQLDALINKLESSDAVQKQKEELEKLNQLLVEKRKAYPAMVQLQFRSEALIIHLRELCEAHQAQMAKTRNVRAQEITNGRWKVQWLTDWVGLTTDERVTLANKEKELAKFKEDLNNDEYDLQELISNLAEKNPSELEEAIGISKESAQKLHKLLTHLNHSTTFMSKIEQRLQSIDELLNEFGKQAPRTEMIKTVEEKQGTLLRL |
| Enzyme Length | 1495 |
| Uniprot Accession Number | Q5ZYX7 |
| Absorption | |
| Active Site | ACT_SITE 64; /note=For deubiquitinase activity; /evidence=ECO:0000250|UniProtKB:Q5ZTK4; ACT_SITE 80; /note=For deubiquitinase activity; /evidence=ECO:0000250|UniProtKB:Q5ZTK4; ACT_SITE 117; /note=Nucleophile; for deubiquitinase activity; /evidence=ECO:0000250|UniProtKB:Q5ZTK4 |
| Activity Regulation | |
| Binding Site | BINDING 857; /note="NAD"; /evidence="ECO:0000250|UniProtKB:P21454, ECO:0000250|UniProtKB:Q5ZTK4" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:142554; EC=2.4.2.31; Evidence={ECO:0000269|PubMed:27049943}; |
| DNA Binding | |
| EC Number | 3.4.22.-; 2.3.2.-; 2.4.2.31 |
| Enzyme Function | FUNCTION: Effector that interferes with the host cell ubiquitin pathway and is required for intracellular bacterial replication. Catalyzes the ubiquitination of several host Rab small GTPases associated with the endoplasmic reticulum during L.pneumophila infection, without engaging the standard cellular enzyme cascade (E1 and E2) (PubMed:27049943). Transfers an ADP-ribose moiety from NAD to the 'Arg-42' residue of ubiquitin in a reaction that releases nicotinamide (PubMed:27049943, PubMed:29731171). The modified ubiquitin is subsequently transferred to serine residues of the substrate protein via a phosphoribose linker that results in the release of AMP (PubMed:27912065). {ECO:0000269|PubMed:27049943, ECO:0000269|PubMed:27912065, ECO:0000269|PubMed:29731171}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 761..767; /note="NAD"; /evidence="ECO:0000250|UniProtKB:P21454, ECO:0000250|UniProtKB:Q5ZTK4" |
| Features | Active site (3); Binding site (1); Chain (1); Erroneous initiation (1); Modified residue (1); Nucleotide binding (1); Region (3) |
| Keywords | Hydrolase;Isopeptide bond;Multifunctional enzyme;NAD;Nucleotide-binding;Protease;Reference proteome;Thiol protease;Transferase;Ubl conjugation pathway;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 855; /note=5-glutamyl glutamate; /evidence=ECO:0000250|UniProtKB:Q5ZTK4 |
| Post Translational Modification | PTM: Glutamylated by SidJ; glutamylation inhibits sidE activity to catalyze the production of ADP-ribosylated ubiquitin. {ECO:0000250|UniProtKB:Q5ZTK4}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 169,413 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:19149 |
| Cross Reference Brenda |