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1.C.10.1.1
Haemolysin E, HlyE (ClyA). A peptide derived from the putative transmembrane domain in the tail region of hemolysin E (aas 88-120) assembles in phospholipid membrane and exhibits lytic activity to human red blood cells (Yadav et al., 2009). Residues important for insertion and activity have been identified (Ludwig et al., 2010).  An unusual assembly pathway has been proposed (see family description; Fahie et al. 2013). The pore can be blocked by PAMAM dendrimers (Mandal et al. 2016).  The C-terminus directs pore formation and function (Sathyanarayana et al. 2016).  Similar in structure to Cry6Aa (TC# 1.C.41.2.1) although sequence similarity could not be discerned (Dementiev et al. 2016 and unpublished results).  The C-terminal domain is not directly involved in the pore structure, but is not a passive player in pore formation as it plays important roles in mediating the transition through intermediary steps leading to successful pore formation in a membrane (Sathyanarayana et al. 2016). Transmembrane oligomeric intermediates or "arcs" probably form stable proteolipidic complexes consisting of protein arcs with toroidal lipids lining the free edges (Desikan et al. 2017).

Accession Number:P77335
Protein Name:HlyE aka HPR aka SHEA aka CLYA aka B1182
Length:303
Molecular Weight:33759.00
Species:Escherichia coli [83333]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Secreted1 / Single-pass membrane protein2
Substrate small molecules

Cross database links:

Genevestigator: P77335
EchoBASE: EB3032
EcoGene: EG13243
eggNOG: NOG72512
HEGENOM: HBG468672
DIP: DIP-9915N
RefSeq: AP_001807.1    NP_415700.4   
Entrez Gene ID: 945745   
Pfam: PF06109   
BioCyc: EcoCyc:G6619-MONOMER    ECOL168927:B1182-MONOMER   
KEGG: ecj:JW5181    eco:b1182   

Gene Ontology

GO:0020002 C:host cell plasma membrane
GO:0016021 C:integral to membrane
GO:0042597 C:periplasmic space
GO:0019835 P:cytolysis
GO:0019836 P:hemolysis by symbiont of host erythrocytes
GO:0006917 P:induction of apoptosis
GO:0009405 P:pathogenesis

References (12)

[1] “The Escherichia coli K-12 sheA gene encodes a 34-kDa secreted haemolysin.”  del Castillo F.J.et.al.   11902713
[2] “Analysis of the SlyA-controlled expression, subcellular localization and pore-forming activity of a 34 kDa haemolysin (ClyA) from Escherichia coli K-12.”  Ludwig A.et.al.   10027972
[3] “A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.”  Oshima T.et.al.   8905232
[4] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[5] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[6] “Molecular analysis of the cytolytic protein ClyA (SheA) from Escherichia coli.”  Oscarsson J.et.al.   10383763
[7] “Vesicle-mediated export and assembly of pore-forming oligomers of the enterobacterial clyA cytotoxin.”  Wai S.N.et.al.   14532000
[8] “Structure-function relationships of a novel bacterial toxin, hemolysin E. The role of alpha G.”  Atkins A.et.al.   11006277
[9] “Silencing and activation of ClyA cytotoxin expression in Escherichia coli.”  Westermark M.et.al.   11053378
[10] “Differential regulation of multiple proteins of Escherichia coli and Salmonella enterica serovar Typhimurium by the transcriptional regulator SlyA.”  Spory A.et.al.   12057949
[11] “Characterization of dominantly negative mutant ClyA cytotoxin proteins in Escherichia coli.”  Wai S.N.et.al.   12949101
[12] “E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy.”  Wallace A.J.et.al.   10660049
Structure:
1QOY   2WCD   4PHO   4PHQ     

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FASTA formatted sequence
1:	MTEIVADKTV EVVKNAIETA DGALDLYNKY LDQVIPWQTF DETIKELSRF KQEYSQAASV 
61:	LVGDIKTLLM DSQDKYFEAT QTVYEWCGVA TQLLAAYILL FDEYNEKKAS AQKDILIKVL 
121:	DDGITKLNEA QKSLLVSSQS FNNASGKLLA LDSQLTNDFS EKSSYFQSQV DKIRKEAYAG 
181:	AAAGVVAGPF GLIISYSIAA GVVEGKLIPE LKNKLKSVQN FFTTLSNTVK QANKDIDAAK 
241:	LKLTTEIAAI GEIKTETETT RFYVDYDDLM LSLLKEAAKK MINTCNEYQK RHGKKTLFEV 
301:	PEV