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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)DescriptionActionsGraphical viewLength
Active sitei363Glycyl thioester intermediateCurated1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
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)DescriptionActionsGraphical viewLength
Mutagenesisi363C → A or S: Loss of ubiquitin ligase activity. 1 Publication1
Mutagenesisi365D → N: Loss of ubiquitin ligase activity, but acts as a thioesterase that uses Cys-363 to hydrolyze the ubiquitin-E2 thioester. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003917541 – 571E3 ubiquitin-protein ligase ipaH3Add BLAST571

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

1571
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 37Combined sources12
Helixi46 – 58Combined sources13
Beta strandi62 – 65Combined sources4
Beta strandi83 – 86Combined sources4
Beta strandi104 – 106Combined sources3
Beta strandi124 – 126Combined sources3
Beta strandi144 – 146Combined sources3
Beta strandi164 – 166Combined sources3
Beta strandi184 – 186Combined sources3
Beta strandi210 – 213Combined sources4
Helixi224 – 228Combined sources5
Beta strandi233 – 236Combined sources4
Beta strandi239 – 241Combined sources3
Helixi244 – 255Combined sources12
Beta strandi263 – 265Combined sources3
Helixi282 – 285Combined sources4
Helixi296 – 301Combined sources6
Turni302 – 305Combined sources4
Helixi309 – 321Combined sources13
Turni322 – 325Combined sources4
Helixi331 – 344Combined sources14
Helixi346 – 358Combined sources13
Helixi367 – 383Combined sources17
Turni384 – 386Combined sources3
Helixi392 – 416Combined sources25
Beta strandi420 – 422Combined sources3
Helixi424 – 435Combined sources12
Turni436 – 440Combined sources5
Beta strandi448 – 450Combined sources3
Helixi458 – 481Combined sources24
Helixi484 – 492Combined sources9
Helixi495 – 504Combined sources10
Helixi543 – 559Combined sources17

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ83RJ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati58 – 81LRR 11 PublicationAdd BLAST24
Repeati83 – 99LRR 21 PublicationAdd BLAST17
Repeati100 – 119LRR 31 PublicationAdd BLAST20
Repeati120 – 144LRR 41 PublicationAdd BLAST25
Repeati146 – 159LRR 51 PublicationAdd BLAST14
Repeati160 – 184LRR 61 PublicationAdd BLAST25
Repeati186 – 202LRR 71 PublicationAdd BLAST17
Repeati205 – 229LRR 81 PublicationAdd BLAST25
Repeati232 – 260LRR 91 PublicationAdd BLAST29

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 260Interaction with target proteinsAdd BLAST260
Regioni269 – 278Linker10
Regioni279 – 571E3 ubiquitin-protein ligase catalytic domainAdd BLAST293

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CVRX-ray2.80A1-571[»]
ProteinModelPortaliQ83RJ4.
SMRiQ83RJ4.
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: November 2, 2016
This is version 82 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.