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Protein

E3 ubiquitin-protein ligase ipaH3

Gene

ipaH3

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 UBE2D1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei363 – 3631Glycyl thioester intermediateCurated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway, Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase ipaH3 (EC:6.3.2.-)
Gene namesi
Name:ipaH3
Ordered Locus Names:SF1383
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
Proteomesi
  • UP000001006 Componenti: Chromosome

Subcellular locationi

  • Secreted By similarity
  • Host cytoplasm By similarity

  • Note: Secreted via Mxi-Spa type III secretion system (TTSS), and delivered into the host cytoplasm.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi363 – 3631C → A or S: Loss of ubiquitin ligase activity. 1 Publication
Mutagenesisi365 – 3651D → N: Loss of ubiquitin ligase activity, but acts as a thioesterase that uses Cys-363 to hydrolyze the ubiquitin-E2 thioester. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 571571E3 ubiquitin-protein ligase ipaH3PRO_0000391754Add
BLAST

Post-translational modificationi

Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme UBE2D3 and ubiquitin.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ83RJ4.

Interactioni

Protein-protein interaction databases

STRINGi198214.SF1383.

Structurei

Secondary structure

1
571
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 3712Combined sources
Helixi46 – 5813Combined sources
Beta strandi62 – 654Combined sources
Beta strandi83 – 864Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi210 – 2134Combined sources
Helixi224 – 2285Combined sources
Beta strandi233 – 2364Combined sources
Beta strandi239 – 2413Combined sources
Helixi244 – 25512Combined sources
Beta strandi263 – 2653Combined sources
Helixi282 – 2854Combined sources
Helixi296 – 3016Combined sources
Turni302 – 3054Combined sources
Helixi309 – 32113Combined sources
Turni322 – 3254Combined sources
Helixi331 – 34414Combined sources
Helixi346 – 35813Combined sources
Helixi367 – 38317Combined sources
Turni384 – 3863Combined sources
Helixi392 – 41625Combined sources
Beta strandi420 – 4223Combined sources
Helixi424 – 43512Combined sources
Turni436 – 4405Combined sources
Beta strandi448 – 4503Combined sources
Helixi458 – 48124Combined sources
Helixi484 – 4929Combined sources
Helixi495 – 50410Combined sources
Helixi543 – 55917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CVRX-ray2.80A1-571[»]
ProteinModelPortaliQ83RJ4.
SMRiQ83RJ4. Positions 280-560.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ83RJ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati58 – 8124LRR 11 PublicationAdd
BLAST
Repeati83 – 9917LRR 21 PublicationAdd
BLAST
Repeati100 – 11920LRR 31 PublicationAdd
BLAST
Repeati120 – 14425LRR 41 PublicationAdd
BLAST
Repeati146 – 15914LRR 51 PublicationAdd
BLAST
Repeati160 – 18425LRR 61 PublicationAdd
BLAST
Repeati186 – 20217LRR 71 PublicationAdd
BLAST
Repeati205 – 22925LRR 81 PublicationAdd
BLAST
Repeati232 – 26029LRR 91 PublicationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 260260Interaction with target proteinsAdd
BLAST
Regioni269 – 27810Linker
Regioni279 – 571293E3 ubiquitin-protein ligase catalytic domainAdd
BLAST

Domaini

The LRR (leucine-rich repeat) domain forms a slightly curved solenoid and may mediate interaction with target proteins.1 Publication

Sequence similaritiesi

Contains 9 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiENOG4108QHK. Bacteria.
COG4886. LUCA.
HOGENOMiHOG000290475.
OMAiTQFPQNL.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR032674. LRR_E3_ligase_N.
IPR029487. NEL_dom.
[Graphical view]
PfamiPF14496. NEL. 1 hit.
PF12468. TTSSLRR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q83RJ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIMLPINNN FSLSQNSFYN TISGTYADYF SAWDKWEKQA LPGENRNEAV
60 70 80 90 100
SLLKECLINQ FSELQLNRLN LSSLPDNLPP QITVLEITQN ALISLPELPA
110 120 130 140 150
SLEYLDACDN RLSTLPELPA SLKHLDVDNN QLTMLPELPA LLEYINADNN
160 170 180 190 200
QLTMLPELPT SLEVLSVRNN QLTFLPELPE SLEALDVSTN LLESLPAVPV
210 220 230 240 250
RNHHSEETEI FFRCRENRIT HIPENILSLD PTCTIILEDN PLSSRIRESL
260 270 280 290 300
SQQTAQPDYH GPRIYFSMSD GQQNTLHRPL ADAVTAWFPE NKQSDVSQIW
310 320 330 340 350
HAFEHEEHAN TFSAFLDRLS DTVSARNTSG FREQVAAWLE KLSTSAELRQ
360 370 380 390 400
QSFAVAADAT ESCEDRVALT WNNLRKTLLV HQASEGLFDN DTGALLSLGR
410 420 430 440 450
EMFRLEILED IARDKVRTLH FVDEIEVYLA FQTMLAEKLQ LSTAVKEMRF
460 470 480 490 500
YGVSGVTAND LRTAEAMVRS REENEFTDWF SLWGPWHAVL KRTEADRWAQ
510 520 530 540 550
AEEQKYEMLE NEYSQRVADR LKASGLSGDA DAEREAGAQV MRETEQQIYR
560 570
QVTDEVLALR LSENGSQLHH S
Length:571
Mass (Da):64,943
Last modified:June 1, 2003 - v1
Checksum:iB0DF655E1540D77D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN42986.1.
RefSeqiNP_707279.1. NC_004337.2.

Genome annotation databases

EnsemblBacteriaiAAN42986; AAN42986; SF1383.
GeneIDi1024395.
KEGGisfl:SF1383.
PATRICi18714819. VBIShiFle86970_1628.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN42986.1.
RefSeqiNP_707279.1. NC_004337.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CVRX-ray2.80A1-571[»]
ProteinModelPortaliQ83RJ4.
SMRiQ83RJ4. Positions 280-560.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF1383.

Proteomic databases

PaxDbiQ83RJ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN42986; AAN42986; SF1383.
GeneIDi1024395.
KEGGisfl:SF1383.
PATRICi18714819. VBIShiFle86970_1628.

Phylogenomic databases

eggNOGiENOG4108QHK. Bacteria.
COG4886. LUCA.
HOGENOMiHOG000290475.
OMAiTQFPQNL.

Miscellaneous databases

EvolutionaryTraceiQ83RJ4.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR032674. LRR_E3_ligase_N.
IPR029487. NEL_dom.
[Graphical view]
PfamiPF14496. NEL. 1 hit.
PF12468. TTSSLRR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIPA3_SHIFL
AccessioniPrimary (citable) accession number: Q83RJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: June 1, 2003
Last modified: September 7, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.