Q83RJ4 · IPA3_SHIFL
- ProteinE3 ubiquitin-protein ligase ipaH3
- GeneipaH3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids571 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Synthesizes a 'Lys-48'-linked ubiquitin chain, which requires non-covalent binding between ubiquitin and the host ubiquitin-conjugating enzyme UBE2D1.
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 363 | Glycyl thioester intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | host cell cytoplasm | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | modulation of process of another organism | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase ipaH3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Shigella
Accessions
- Primary accessionQ83RJ4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 363 | Loss of ubiquitin ligase activity. | ||||
Sequence: C → A or S | ||||||
Mutagenesis | 365 | Loss of ubiquitin ligase activity, but acts as a thioesterase that uses Cys-363 to hydrolyze the ubiquitin-E2 thioester. | ||||
Sequence: D → N |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000391754 | 1-571 | E3 ubiquitin-protein ligase ipaH3 | |||
Sequence: MSIMLPINNNFSLSQNSFYNTISGTYADYFSAWDKWEKQALPGENRNEAVSLLKECLINQFSELQLNRLNLSSLPDNLPPQITVLEITQNALISLPELPASLEYLDACDNRLSTLPELPASLKHLDVDNNQLTMLPELPALLEYINADNNQLTMLPELPTSLEVLSVRNNQLTFLPELPESLEALDVSTNLLESLPAVPVRNHHSEETEIFFRCRENRITHIPENILSLDPTCTIILEDNPLSSRIRESLSQQTAQPDYHGPRIYFSMSDGQQNTLHRPLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSTSAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYSQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQVTDEVLALRLSENGSQLHHS |
Post-translational modification
Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme UBE2D3 and ubiquitin.
Keywords
- PTM
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-260 | Interaction with target proteins | ||||
Sequence: MSIMLPINNNFSLSQNSFYNTISGTYADYFSAWDKWEKQALPGENRNEAVSLLKECLINQFSELQLNRLNLSSLPDNLPPQITVLEITQNALISLPELPASLEYLDACDNRLSTLPELPASLKHLDVDNNQLTMLPELPALLEYINADNNQLTMLPELPTSLEVLSVRNNQLTFLPELPESLEALDVSTNLLESLPAVPVRNHHSEETEIFFRCRENRITHIPENILSLDPTCTIILEDNPLSSRIRESLSQQTAQPDYH | ||||||
Repeat | 58-81 | LRR 1 | ||||
Sequence: INQFSELQLNRLNLSSLPDNLPPQ | ||||||
Repeat | 83-99 | LRR 2 | ||||
Sequence: TVLEITQNALISLPELP | ||||||
Repeat | 100-119 | LRR 3 | ||||
Sequence: ASLEYLDACDNRLSTLPELP | ||||||
Repeat | 120-144 | LRR 4 | ||||
Sequence: ASLKHLDVDNNQLTMLPELPALLEY | ||||||
Repeat | 146-159 | LRR 5 | ||||
Sequence: NADNNQLTMLPELP | ||||||
Repeat | 160-184 | LRR 6 | ||||
Sequence: TSLEVLSVRNNQLTFLPELPESLEA | ||||||
Repeat | 186-202 | LRR 7 | ||||
Sequence: DVSTNLLESLPAVPVRN | ||||||
Repeat | 205-229 | LRR 8 | ||||
Sequence: SEETEIFFRCRENRITHIPENILSL | ||||||
Repeat | 232-260 | LRR 9 | ||||
Sequence: TCTIILEDNPLSSRIRESLSQQTAQPDYH | ||||||
Region | 269-278 | Linker | ||||
Sequence: SDGQQNTLHR | ||||||
Region | 279-571 | E3 ubiquitin-protein ligase catalytic domain | ||||
Sequence: PLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSTSAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYSQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQVTDEVLALRLSENGSQLHHS | ||||||
Domain | 287-497 | NEL | ||||
Sequence: WFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSTSAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADR |
Domain
The LRR (leucine-rich repeat) domain forms a slightly curved solenoid and may mediate interaction with target proteins.
Sequence similarities
Belongs to the LRR-containing bacterial E3 ligase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length571
- Mass (Da)64,943
- Last updated2003-06-01 v1
- ChecksumB0DF655E1540D77D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE005674 EMBL· GenBank· DDBJ | AAN42986.1 EMBL· GenBank· DDBJ | Genomic DNA |