Descriptions

Autoinhibition of SlrP, a type III secretion system effector from the NEL family, involves structural constraints that sequester the NEL domain. These constraints are proposed to be sequentially released upon interaction with host substrates, leading to E3 ubiquitin ligase activity modulation.

Autoinhibitory domains (AIDs)

Target domain

465-765 (NEL domain)

Relief mechanism

PTM

Assay

Structural analysis

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

2 structures for D0ZRB2

Entry ID Method Resolution Chain Position Source
4PUF X-ray 330 A A/B 141-765 PDB
AF-D0ZRB2-F1 Predicted AlphaFoldDB

No variants for D0ZRB2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for D0ZRB2

No associated diseases with D0ZRB2

8 regional properties for D0ZRB2

Type Name Position InterPro Accession
repeat Leucine-rich repeat 263 - 284 IPR001611
repeat Leucine-rich repeat, typical subtype 199 - 220 IPR003591-1
repeat Leucine-rich repeat, typical subtype 260 - 284 IPR003591-2
repeat Leucine-rich repeat, typical subtype 302 - 326 IPR003591-3
repeat Leucine-rich repeat, typical subtype 346 - 368 IPR003591-4
repeat Leucine-rich repeat, typical subtype 370 - 389 IPR003591-5
domain Novel E3 ligase domain 472 - 680 IPR029487
domain LRR-containing bacterial E3 ligase, N-terminal 107 - 170 IPR032674

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Secreted
  • Host cytoplasm
  • Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 T3SS), and delivered into the host cytoplasm
PANTHER Family PTHR47114 FAMILY NOT NAMED
PANTHER Subfamily PTHR47114:SF2 OLIGODENDROCYTE-MYELIN GLYCOPROTEIN
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 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 cytoplasm The cytoplasm of a host cell.

2 GO annotations of molecular function

Name Definition
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond
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.

3 GO annotations of biological process

Name Definition
killing of cells of another organism Any process in an organism that results in the killing of cells of another organism, including in some cases the death of the other organism. Killing here refers to the induction of death in one cell by another cell, not cell-autonomous death due to internal or other environmental conditions.
protein secretion by the type III secretion system The process in which proteins are transferred into the extracellular milieu or directly into host cells by the bacterial type III secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
protein ubiquitination The process in which one or more ubiquitin groups are 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
MFNITNIQST ARHQSISNEA STEVPLKEEI WNKISAFFSS EHQVEAQNCI AYLCHPPETA
70 80 90 100 110 120
SPEEIKSKFE CLRMLAFPAY ADNIQYSRGG ADQYCILSEN SQEILSIVFN TEGYTVEGGG
130 140 150 160 170 180
KSVTYTRVTE SEQASSASGS KDAVNYELIW SEWVKEAPAK EAANREEAVQ RMRDCLKNNK
190 200 210 220 230 240
TELRLKILGL TTIPAYIPEQ ITTLILDNNE LKSLPENLQG NIKTLYANSN QLTSIPATLP
250 260 270 280 290 300
DTIQEMELSI NRITELPERL PSALQSLDLF HNKISCLPEN LPEELRYLSV YDNSIRTLPA
310 320 330 340 350 360
HLPSEITHLN VQSNSLTALP ETLPPGLKTL EAGENALTSL PASLPPELQV LDVSKNQITV
370 380 390 400 410 420
LPETLPPTIT TLDVSRNALT NLPENLPAAL QIMQASRNNL VRLPESLPHF RGEGPQPTRI
430 440 450 460 470 480
IVEYNPFSER TIQNMQRLMS SVDYQGPRVL FAMGDFSIVR VTRPLHQAVQ GWLTSLEEED
490 500 510 520 530 540
VNQWRAFEAE ANAAAFSGFL DYLGDTQNTR HPDFKEQVSA WLMRLAEDSA LRETVFIIAM
550 560 570 580 590 600
NATISCEDRV TLAYHQMQEA TLVHDAERGA FDSHLAELIM AGREIFRLEQ IESLAREKVK
610 620 630 640 650 660
RLFFIDEVEV FLGFQNQLRE SLSLTTMTRD MRFYNVSGIT ESDLDEAEIR IKMAENRDFH
670 680 690 700 710 720
KWFALWGPWH KVLERIAPEE WREMMAKRDE CIETDEYQSR VNAELEDLRI ADDSDAERTT
730 740 750 760
EVQMDAERAI GIKIMEEINQ TLFTEIMENI LLKKEVSSLM SAYWR