P0CE12

EV
Gene name
sspH2 (STM2241)
Protein name
E3 ubiquitin-protein ligase SspH2
Names
RING-type E3 ubiquitin transferase SspH2, Salmonella secreted protein H2, Secreted effector protein sspH2
Species
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
KEGG Pathway
stm:STM2241
EC number
2.3.2.27: Aminoacyltransferases
Protein Class
FAMILY NOT NAMED (PTHR47114)

Descriptions

SspH2, consisting of an LRR domain and a Novel E3 ligase (NEL) domain, is an E3 ubiquitin ligase with unique folding. The NEL domain has a catalytic activity that is inhibited by the LRR domain by sequestering the catalytic cysteine residue contained in the NEL domain. The N-terminal domain targets SspH2 to the apical plasma membrane of polarized epithelial cells, which is expected to play a role in releasing the ligase domain for site-specific function.

Autoinhibitory domains (AIDs)

223-466 (LRR domain) EV

Target domain

502-712 (Novel E3 ligase, NEL domain)

Relief mechanism

Partner binding

Assay

Mutagenesis experiment, Structural analysis

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

2 structures for P0CE12

Entry ID Method Resolution Chain Position Source
3G06 X-ray 190 A A 166-783 PDB
AF-P0CE12-F1 Predicted AlphaFoldDB

No variants for P0CE12

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0CE12

No associated diseases with P0CE12

10 regional properties for P0CE12

Type Name Position InterPro Accession
repeat Leucine-rich repeat 243 - 264 IPR001611-1
repeat Leucine-rich repeat 303 - 324 IPR001611-2
repeat Leucine-rich repeat 343 - 364 IPR001611-3
repeat Leucine-rich repeat 383 - 404 IPR001611-4
repeat Leucine-rich repeat, typical subtype 242 - 267 IPR003591-1
repeat Leucine-rich repeat, typical subtype 302 - 327 IPR003591-2
repeat Leucine-rich repeat, typical subtype 340 - 367 IPR003591-3
repeat Leucine-rich repeat, typical subtype 380 - 403 IPR003591-4
repeat Leucine-rich repeat, typical subtype 420 - 444 IPR003591-5
domain Novel E3 ligase domain 502 - 714 IPR029487

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Secreted
  • Host cytoplasm
  • Host apical cell membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Secreted via type III secretion system 2 (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

4 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.
host cell plasma membrane The plasma membrane surrounding a host cell.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

3 GO annotations of molecular function

Name Definition
catalytic activity Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
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: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
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.

5 GO annotations of biological process

Name Definition
positive regulation of interleukin-8 production Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway Any process that activates or increases the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing 1 (NOD1) pathway.
positive regulation of plant-type hypersensitive response Any process that activates or increases the frequency, rate or extent of the hypersensitive response in a plant.
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
MPFHIGSGCL PATISNRRIY RIAWSDTPPE MSSWEKMKEF FCSTHQTEAL ECIWTICHPP
70 80 90 100 110 120
AGTTREDVIN RFELLRTLAY AGWEESIHSG QHGENYFCIL DEDSQEILSV TLDDAGNYTV
130 140 150 160 170 180
NCQGYSETHR LTLDTAQGEE GTGHAEGASG TFRTSFLPAT TAPQTPAEYD AVWSAWRRAA
190 200 210 220 230 240
PAEESRGRAA VVQKMRACLN NGNAVLNVGE SGLTTLPDCL PAHITTLVIP DNNLTSLPAL
250 260 270 280 290 300
PPELRTLEVS GNQLTSLPVL PPGLLELSIF SNPLTHLPAL PSGLCKLWIF GNQLTSLPVL
310 320 330 340 350 360
PPGLQELSVS DNQLASLPAL PSELCKLWAY NNQLTSLPML PSGLQELSVS DNQLASLPTL
370 380 390 400 410 420
PSELYKLWAY NNRLTSLPAL PSGLKELIVS GNRLTSLPVL PSELKELMVS GNRLTSLPML
430 440 450 460 470 480
PSGLLSLSVY RNQLTRLPES LIHLSSETTV NLEGNPLSER TLQALREITS APGYSGPIIR
490 500 510 520 530 540
FDMAGASAPR ETRALHLAAA DWLVPAREGE PAPADRWHMF GQEDNADAFS LFLDRLSETE
550 560 570 580 590 600
NFIKDAGFKA QISSWLAQLA EDEALRANTF AMATEATSSC EDRVTFFLHQ MKNVQLVHNA
610 620 630 640 650 660
EKGQYDNDLA ALVATGREMF RLGKLEQIAR EKVRTLALVD EIEVWLAYQN KLKKSLGLTS
670 680 690 700 710 720
VTSEMRFFDV SGVTVTDLQD AELQVKAAEK SEFREWILQW GPLHRVLERK APERVNALRE
730 740 750 760 770 780
KQISDYEETY RMLSDTELRP SGLVGNTDAE RTIGARAMES AKKTFLDGLR PLVEEMLGSY
LNVQWRRN