Descriptions

Shigellar flexneri IpaH9.8 E3 ligase inhibits MAPK kinase dependent signaling by targeting components of this pathway and disrupts both NF-觀B-dependent gene expression and the activity of U2AF35 via the ubiquitination. The C-terminal region of IpaH9.8 can exist as a monomer able to catalyse the ubiquitination of U2AF35 and as a dimer that does not possess this activity. Under non-reducing conditions, the sole cysteine of the C-terminal region of IpaH9.8 forms an intermolecular disulfide bridge resulting in the extension of an α-helix and formation of a domain-swapped dimer. Furthermore, the N-terminal domain (leucine-rich repeat) may be inhibitory for the autoinhibition activity of the full-length IpaH9.8 and substrate (human substrate U2AF35) binding releases this inhibition.

Autoinhibitory domains (AIDs)

Target domain

261-471 (E3 ubiquitin-protein ligase catalytic domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q326Z6

Entry ID Method Resolution Chain Position Source
AF-Q326Z6-F1 Predicted AlphaFoldDB

No variants for Q326Z6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q326Z6

No associated diseases with Q326Z6

2 regional properties for Q326Z6

Type Name Position InterPro Accession
domain Novel E3 ligase domain 261 - 471 IPR029487
domain LRR-containing bacterial E3 ligase, N-terminal 4 - 48 IPR032674

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Secreted
  • Host cytoplasm
  • Host nucleus
  • Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm
  • Transported into the host nucleus
  • This transport is independent of cytosolic factors, but dependent on temperature and partly on ATP/GTP
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
host cell cytosol The part of the host cell cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
host cell nucleus A membrane-bounded organelle as it is found in the host cell in which chromosomes are housed and replicated. The host is defined as the larger of the organisms involved in a symbiotic interaction.

1 GO annotations of molecular function

Name Definition
ubiquitin-protein transferase activity Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.

1 GO annotations of biological process

Name Definition
protein K27-linked ubiquitination A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 27 of the ubiquitin monomers, is added to a protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLPINNNFSL PQNSFYNTIS GTYADYFSAW DKWEKQALPG EERDEAVSRL KECLINNSDE
70 80 90 100 110 120
LRLDRLNLSS LPDNLPAQIT LLNVSYNQLT NLPELPVTLK KLYSASNKLS ELPVLPPALE
130 140 150 160 170 180
SLQVQHNELE NLPALPDSLL TMNISYNEIV SLPSLPQALK NLRATRNFLT ELPAFSEGNN
190 200 210 220 230 240
PVVREYFFDR NQISHIPESI LNLRNECSIH ISDNPLSSHA LQALQRLTSS PDYHGPRIYF
250 260 270 280 290 300
SMSDGQQNTL HRPLADAVTA WFPENKQSDV SQTWHAFEHE EHANTFSAFL DRLSDTVSAR
310 320 330 340 350 360
NTSGFREQVA AWLEKLSASA ELRQQSFAVA ADATESCEDR VALTWNNLRK TLLVHQASEG
370 380 390 400 410 420
LFDNDTGALL SLGREMFRLE ILEDIARDKV RTLHFVDEIE VYLAFQTMLA EKLQLSTAVK
430 440 450 460 470 480
EMRFYGVSGV TANDLRTAEA MVRSREENEF TDWFSLWGPW HAVLKRTEAD RWALAEEQKY
490 500 510 520 530 540
EMLENEYPQR VADRLKASGL SGDADAEREA GAQVMRETEQ QIYRQLTDEV LALRLSENGS
QLHHS