P18011 · SCTE_SHIFL
- ProteinType 3 secretion system translocon protein SctE
- GenesctE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids580 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:10545510, PubMed:17367391).
IpaB/SctE and IpaC/SctB are inserted into the host membrane where they form a pore and allow the translocation of effector proteins into the cytosol of target cells (PubMed:10545510, PubMed:17367391, PubMed:34809452).
Interaction with IpaD/SctA at needle tips leads to the formation of the MxiH/SctF-IpaD/SctA-IpaB/SctE ternary complex, which is essential for host cell sensing (PubMed:17367391, PubMed:19433542).
Interaction of IpaB/SctE with host membrane lipids promotes recruitment of IpaC/SctB at the needle tip concomitant with translocon insertion into the host membrane and type III secretion induction (PubMed:19433542).
IpaB/SctE and IpaC/SctB are inserted into the host membrane where they form a pore and allow the translocation of effector proteins into the cytosol of target cells (PubMed:10545510, PubMed:17367391, PubMed:34809452).
Interaction with IpaD/SctA at needle tips leads to the formation of the MxiH/SctF-IpaD/SctA-IpaB/SctE ternary complex, which is essential for host cell sensing (PubMed:17367391, PubMed:19433542).
Interaction of IpaB/SctE with host membrane lipids promotes recruitment of IpaC/SctB at the needle tip concomitant with translocon insertion into the host membrane and type III secretion induction (PubMed:19433542).
Required for efficient dissemination (PubMed:11207551).
Necessary for lysis of the two cellular membranes that surround bacteria in protrusions during cell-to-cell spread (PubMed:11207551).
Is sufficient to induce macrophage apoptosis through activation of the interleukin-1 beta converting enzyme (ICE) in infected macrophages (PubMed:8670890, PubMed:9009343).
In epithelial cells, causes cell-cycle arrest by targeting host MAD2L2, an anaphase-promoting complex/cyclosome (APC) inhibitor (PubMed:17719540).
Necessary for lysis of the two cellular membranes that surround bacteria in protrusions during cell-to-cell spread (PubMed:11207551).
Is sufficient to induce macrophage apoptosis through activation of the interleukin-1 beta converting enzyme (ICE) in infected macrophages (PubMed:8670890, PubMed:9009343).
In epithelial cells, causes cell-cycle arrest by targeting host MAD2L2, an anaphase-promoting complex/cyclosome (APC) inhibitor (PubMed:17719540).
Activity regulation
Interaction with the membrane is affected by the pH (PubMed:10971588).
IpaB/SctE is more efficient in destabilizing the membrane at pH 5.0 than at neutral pH (PubMed:10971588).
IpaB/SctE is more efficient in destabilizing the membrane at pH 5.0 than at neutral pH (PubMed:10971588).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | host cell | |
Cellular Component | host cell membrane | |
Cellular Component | host cell nucleus | |
Cellular Component | membrane |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameType 3 secretion system translocon protein SctE
- Short namesT3SS translocon protein SctE
- Alternative names
Gene names
Encoded on
- Plasmid pWR100
- Plasmid pWR501
- Plasmid pMYSH6000
- Plasmid pCP301
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Shigella
Accessions
- Primary accessionP18011
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Host membrane ; Multi-pass membrane protein
Note: Secreted via the type III secretion system (T3SS) (PubMed:10545510).
Localizes at the surface of needle tips via IpaD/SctA (PubMed:17367391).
IpaB/SctE and IpaC/SctB form a multimeric integral membrane complex in eukaryotic cell membranes (PubMed:10545510, PubMed:17367391).
Also secreted into the cytoplasm of the infected macrophage after the escape of bacteria from phagosome, where it colocalizes with ICE (PubMed:8670890, PubMed:9009343).
May localize to host cell nucleus during G2/M phase of the host cell cycle (PubMed:17719540).
Localizes at the surface of needle tips via IpaD/SctA (PubMed:17367391).
IpaB/SctE and IpaC/SctB form a multimeric integral membrane complex in eukaryotic cell membranes (PubMed:10545510, PubMed:17367391).
Also secreted into the cytoplasm of the infected macrophage after the escape of bacteria from phagosome, where it colocalizes with ICE (PubMed:8670890, PubMed:9009343).
May localize to host cell nucleus during G2/M phase of the host cell cycle (PubMed:17719540).
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 313-333 | Helical | ||||
Sequence: ILGALLTIVSVVAAAFSGGAS | ||||||
Transmembrane | 399-419 | Helical | ||||
Sequence: IGSILGAIAGALVLVAAVVLV |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Deletion mutant shows fast constitutive secretion and displays increased adhesion to HeLa cells (PubMed:20086081).
Mutant is non-hemolytic in the presence of sheep red blood cell (RBC) (PubMed:10545510, PubMed:20086081).
Mutant displays normal secretons (PubMed:10545510).
Mutant is non-hemolytic in the presence of sheep red blood cell (RBC) (PubMed:10545510, PubMed:20086081).
Mutant displays normal secretons (PubMed:10545510).
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 18 | in plasmid pMYSH6000 and plasmid pCP301 | ||||
Sequence: T → A | ||||||
Mutagenesis | 61 | Loss of interaction with human MAD2L2. | ||||
Sequence: N → A | ||||||
Mutagenesis | 572-580 | Shows fast constitutive secretion. Partially invasive and hyperadhesive. Can still form pores by inserting itself and IpaC/SctB into membranes, but is completely unable to lyse red blood cells. Does not affect the ability of Shigella to lyse the epithelial cell invasion vacuole. Affects IpaB/SctE ability to bind needle tips and leads to increased IpaC/SctB recruitment to purified needles. | ||||
Sequence: Missing | ||||||
Mutagenesis | 578-580 | Shows fast constitutive secretion. Partially invasive and hyperadhesive. Can still form pores by inserting itself and IpaC/SctB into membranes, but is completely unable to lyse red blood cells. Does not affect the ability of Shigella to lyse the epithelial cell invasion vacuole. Affects IpaB/SctE ability to bind needle tips and leads to increased IpaC/SctB recruitment to purified needles. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000219853 | 1-580 | Type 3 secretion system translocon protein SctE | |||
Sequence: MHNVSTTTTGFPLAKILTSTELGDNTIQAANDAANKLFSLTIADLTANQNINTTNAHSTSNILIPELKAPKSLNASSQLTLLIGNLIQILGEKSLTALTNKITAWKSQQQARQQKNLEFSDKINTLLSETEGLTRDYEKQINKLKNADSKIKDLENKINQIQTRLSELDPESPEKKKLSREEIQLTIKKDAAVKDRTLIEQKTLSIHSKLTDKSMQLEKEIDSFSAFSNTASAEQLSTQQKSLTGLASVTQLMATFIQLVGKNNEESLKNDLALFQSLQESRKTEMERKSDEYAAEVRKAEELNRVMGCVGKILGALLTIVSVVAAAFSGGASLALAAVGLALMVTDAIVQAATGNSFMEQALNPIMKAVIEPLIKLLSDAFTKMLEGLGVDSKKAKMIGSILGAIAGALVLVAAVVLVATVGKQAAAKLAENIGKIIGKTLTDLIPKFLKNFSSQLDDLITNAVARLNKFLGAAGDEVISKQIISTHLNQAVLLGESVNSATQAGGSVASAVFQNSASTNLADLTLSKYQVEQLSKYISEAIEKFGQLQEVIADLLASMSNSQANRTDVAKAILQQTTA |
Proteomic databases
Expression
Induction
Synthesis of this immunogen is repressed at 30 degrees Celsius and restored at 37 degrees Celsius.
Interaction
Subunit
The core secretion machinery of the T3SS is composed of approximately 20 different proteins, including cytoplasmic components, a base, an export apparatus and a needle (PubMed:30107569).
This subunit is involved in the formation of a pore, called the translocon, in host membrane (PubMed:10545510, PubMed:17367391, PubMed:34809452).
Interacts with IpaC/SctB (PubMed:10545510, PubMed:17367391, PubMed:7954817).
Interacts with the needle tip protein IpaD/SctA (PubMed:17367391, PubMed:24236510).
Interacts with the molecular chaperone IpgC, which prevents premature association with IpaC/SctB within the cytoplasm of Shigella cells and protects IpaB/SctE from proteolysis (PubMed:11207551, PubMed:19478065, PubMed:20937829, PubMed:7954817).
Interacts with the host protein ICE in the cytoplasm of infected macrophages (PubMed:8670890).
Interacts with human MAD2L2 in the G2/M phase of the cell cycle (PubMed:17719540, PubMed:31484720).
This subunit is involved in the formation of a pore, called the translocon, in host membrane (PubMed:10545510, PubMed:17367391, PubMed:34809452).
Interacts with IpaC/SctB (PubMed:10545510, PubMed:17367391, PubMed:7954817).
Interacts with the needle tip protein IpaD/SctA (PubMed:17367391, PubMed:24236510).
Interacts with the molecular chaperone IpgC, which prevents premature association with IpaC/SctB within the cytoplasm of Shigella cells and protects IpaB/SctE from proteolysis (PubMed:11207551, PubMed:19478065, PubMed:20937829, PubMed:7954817).
Interacts with the host protein ICE in the cytoplasm of infected macrophages (PubMed:8670890).
Interacts with human MAD2L2 in the G2/M phase of the cell cycle (PubMed:17719540, PubMed:31484720).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P18011 | Casp1 P29452 | 3 | EBI-490239, EBI-489700 | |
XENO | P18011 | CD44 P16070 | 4 | EBI-490239, EBI-490245 | |
BINARY | P18011 | ipgC P0A2U4 | 4 | EBI-490239, EBI-1535618 | |
XENO | P18011 | MAD2L2 Q9UI95 | 7 | EBI-490239, EBI-77889 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 15-45 | IpgC chaperone binding domain 1 | ||||
Sequence: KILTSTELGDNTIQAANDAANKLFSLTIADL | ||||||
Region | 51-72 | IpgC chaperone binding domain 2 | ||||
Sequence: INTTNAHSTSNILIPELKAPKS | ||||||
Region | 61-70 | Mediates interaction with human MAD2L2 | ||||
Sequence: NILIPELKAP | ||||||
Coiled coil | 104-224 | |||||
Sequence: AWKSQQQARQQKNLEFSDKINTLLSETEGLTRDYEKQINKLKNADSKIKDLENKINQIQTRLSELDPESPEKKKLSREEIQLTIKKDAAVKDRTLIEQKTLSIHSKLTDKSMQLEKEIDSF |
Domain
The immediate N-terminus is needed for recognition by the secretion apparatus and chaperone binding (PubMed:29672980).
The N-terminal region is necessary for interaction with IpaD/SctA and the sequential maturation of the T3SS needle tip (PubMed:24236510).
The C-terminal half is key to the activities needed for formation of an active translocon and possibly for translocation itself (PubMed:29672980).
The extreme C-terminus is required for efficient needle tip binding, and its absence also affects regulation of secretion and adhesion to and possibly invasion of host cells (PubMed:20086081).
Portion of the translocon pore channel adopts a funnel-like conformation, wherein it narrows toward the cytosolic side of the plasma membrane (PubMed:34809452).
The N-terminal region is necessary for interaction with IpaD/SctA and the sequential maturation of the T3SS needle tip (PubMed:24236510).
The C-terminal half is key to the activities needed for formation of an active translocon and possibly for translocation itself (PubMed:29672980).
The extreme C-terminus is required for efficient needle tip binding, and its absence also affects regulation of secretion and adhesion to and possibly invasion of host cells (PubMed:20086081).
Portion of the translocon pore channel adopts a funnel-like conformation, wherein it narrows toward the cytosolic side of the plasma membrane (PubMed:34809452).
Sequence similarities
Belongs to the SctE/SipB/YopB family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length580
- Mass (Da)62,201
- Last updated1994-02-01 v2
- Checksum56325105E4BC0F70
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 167 | in Ref. 2; AAA26522 | ||||
Sequence: E → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J04117 EMBL· GenBank· DDBJ | AAA26522.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M34849 EMBL· GenBank· DDBJ | AAA98424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL391753 EMBL· GenBank· DDBJ | CAC05803.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF348706 EMBL· GenBank· DDBJ | AAK18446.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X15319 EMBL· GenBank· DDBJ | CAA33381.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF386526 EMBL· GenBank· DDBJ | AAL72352.1 EMBL· GenBank· DDBJ | Genomic DNA |