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1.C.41.1.3
The non-hemolytic pore-forming cyto-enterotoxin, Nhe (Fagerlund et al., 2008; Sastalla et al. 2013), a three-partite toxin.  Pore formation and subsequent lysis of target cells caused by Nhe is an orchestrated process comprising three steps: (i) formation of NheB/C oligomers in solution, (ii) attachment of the oligomers to the cell membrane, (iii) binding of NheA to the oligomers (Fox et al. 2020). The benefit of these complexes is more stable cell binding as well as stronger and earlier cytotoxic effects. High molecular mass hetero-oligomers (~620 kDa), probably consist of one NheC and up to 15 NheB. NheBC induces membrane permeability. Formation of stable transmembrane channels with a conductance of about 870 pS and a diameter of about 2 nm due to the application of NheBC could be demonstrated in lipid bilayer experiments (Zhu et al. 2015). Thus, the NheBC complex increases the membrane permeability prior to the emergence of full pores containing also NheA. NHE can induce apoptosis (Liu et al. 2016) and activates the NLRP3 inflammasome (Sastalla et al. 2013), a three-partite toxin.  Pore formation and subsequent lysis of target cells caused by Nhe is an orchestrated process comprising three steps: (i) formation of NheB/C oligomers in solution, (ii) attachment of the oligomers to the cell membrane, (iii) binding of NheA to the oligomers (Fox et al. 2020). The benefit of these complexes is more stable cell binding as well as stronger and earlier cytotoxic effects. High molecular mass hetero-oligomers (~620 kDa), probably consist of one NheC and up to 15 NheB. NheBC induces membrane permeability. Formation of stable transmembrane channels with a conductance of about 870 pS and a diameter of about 2 nm due to the application of NheBC could be demonstrated in lipid bilayer experiments (Zhu et al. 2015). Thus, the NheBC complex increases the membrane permeability prior to the emergence of full pores containing also NheA. NHE can induce apoptosis (Liu et al. 2016) and activates the NLRP3 inflammasome (Fox et al. 2020).  

Accession Number:Q2TM55
Protein Name:NheC
Length:359
Molecular Weight:39794.00
Species:Bacillus cereus [1396]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate Solutes

Cross database links:

Pfam: PF05791   

Gene Ontology

GO:0016020 C:membrane
GO:0009405 P:pathogenesis

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MQKRFYKKCL LAVMIAGVAT SNAFPLHPFA AEQNVQVLQE NVKNYSLGPA GFPDVMAPTT 
61:	SSIFAVDSYA KLIQNQQETD LSKISSINSE FKGNMIQPQR DAKINAAYWL NNMKPQIMKT 
121:	DQNIINYNNT FQSYYNDMLI AIDQKDSGKL KADLEKLYAD IVKNQNEVDG LLGNLKAFRD 
181:	RMAKDTNSFK EDTNQLTAIL ASTNAGIPAL EQQINTYNDS IKKSNDMVIA GGVLCVALIT 
241:	CLAGGPMIAV AKKDIANAER EIANLKDRIS GAQAEVVILT DVKNKTTNMT ETIDAAITAL 
301:	QNISNQWYTV GAKYNNLLQN VKGISPEEFT FIKEDLHTAK DSWKDVKDYT EKLHEGVAK