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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:Q63CS3
Protein Name:Nhe-L1
Length:402
Molecular Weight:43117.00
Species:Bacillus cereus (strain ZK / E33L) [288681]
Number of TMSs:3
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate Solutes

Cross database links:

HEGENOM: HBG339049
RefSeq: YP_083294.1   
Entrez Gene ID: 3025133   
Pfam: PF05791   
BioCyc: BCER288681:BCE33L1699-MONOMER   
KEGG: bcz:BCZK1699   

Gene Ontology

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

References (1)

[1] “Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis.”  Han C.S.et.al.   16621833

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MTKKPYKVMA LSALMAVFAA GNIMPAHTYA AESTVKQAPV HAVAKAYNDY EEYSLGPEGL 
61:	KDAMERTGSN ALVMDLYALT IIKQGNVNFG NVSTVDAALK GKVIQHQDTA RGNAKQWLDV 
121:	LKPQLISTNQ NIINYNTKFQ NYYDTLVAAV DAKDKATLTK GLTRLSSSIN ENKAQVDQLV 
181:	EDLKKFRNKM TSDTQNFKGD ANQITSILAS QDAGIPLLQN QITTYNEAIS KYNAIIIGSS 
241:	VATALGPIAI IGGAVVIATG AGTPLGVALI AGGAAAVGGG TAGIVLAKKE LDNAQAEIQK 
301:	ITGQITTAQL EVAGLTNIKT QTEYLTNTID TAITALQNIS NQWYTMGSKY NSLLQNVDSI 
361:	SPNDLVFIKE DLNIAKDSWK NIKDYAEKIY AEDIKVVDTK KA