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1.C.11.1.3
Haemolysin A, HlyA (α-haemolysin) (Wiles and Mulvey 2013). The channel-forming domain may contain β-strands, possibly in addition to alpha-helical structures (Benz et al. 2014).  Although homologous, HlyA and CyaA (1.C.11.1.4) exhibit different modes of permeabilization (Fiser and Konopásek 2009). HlyA triggered an increase in mitochondrial Ca2+ levels and manipulated mitochondrial dynamics by causing fragmentation of the mitochondrial network. Alterations in mitochondrial dynamics resulted in severe impairment of mitochondrial functions by loss of membrane potential, increase in reactive oxygen species production, and ATP depletion. HlyA also caused disruption of plasma membrane integrity (Lu et al. 2018). Cholesterol catalyzes unfolding in membrane inserted motifs of the pore forming cytolysin A (Kulshrestha et al. 2023).

Accession Number:P09983
Protein Name:HLY1 aka HlyA
Length:1023
Molecular Weight:109867.00
Species:Escherichia coli [562]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Secreted1 / Multi-pass membrane protein2
Substrate molecule, calcium ion

Cross database links:

DIP: DIP-16932N
Pfam: PF00353    PF02382    PF08339   

Gene Ontology

GO:0020002 C:host cell plasma membrane
GO:0016021 C:integral to membrane
GO:0005509 F:calcium ion binding
GO:0019835 P:cytolysis
GO:0019836 P:hemolysis by symbiont of host erythrocytes
GO:0009405 P:pathogenesis

References (3)

[1] “Nucleotide sequence of an Escherichia coli chromosomal hemolysin.”  Felmlee T.et.al.   3891743
[2] “Characterisation of HlyC and mechanism of activation and secretion of haemolysin from E. coli 2001.”  Nicaud J.-M.et.al.   3894051
[3] “Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin.”  Stanley P.et.al.   7801126

External Searches:

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MPTITAAQIK STLQSAKQSA ANKLHSAGQS TKDALKKAAE QTRNAGNRLI LLIPKDYKGQ 
61:	GSSLNDLVRT ADELGIEVQY DEKNGTAITK QVFGTAEKLI GLTERGVTIF APQLDKLLQK 
121:	YQKAGNKLGG SAENIGDNLG KAGSVLSTFQ NFLGTALSSM KIDELIKKQK SGGNVSSSEL 
181:	AKASIELINQ LVDTAASLNN VNSFSQQLNK LGSVLSNTKH LNGVGNKLQN LPNLDNIGAG 
241:	LDTVSGILSA ISASFILSNA DADTGTKAAA GVELTTKVLG NVGKGISQYI IAQRAAQGLS 
301:	TSAAAAGLIA SVVTLAISPL SFLSIADKFK RANKIEEYSQ RFKKLGYDGD SLLAAFHKET 
361:	GAIDASLTRI STVLASVSSG ISAAATTSLV GAPVSALVGA VTGIISGILE ASKQAMFEHV 
421:	ASKMADVIAE WEKKHGKNYF ENGYDARHAA FLEDNFKILS QYNKEYSVER SVLITQQHWD 
481:	TLIGELAGVT RNGDKTLSGK SYIDYYEEGK RLEKKPDEFQ KQVFDPLKGN IDLSDSKSST 
541:	LLKFVTPLLT PGEEIRERRQ SGKYEYITEL LVKGVDKWTV KGVQDKGSVY DYSNLIQHAS 
601:	VGNNQYREIR IESHLGDGDD KVFLSAGSAN IYAGKGHDVV YYDKTDTGYL TIDGTKATEA 
661:	GNYTVTRVLG GDVKVLQEVV KEQEVSVGKR TEKTQYRSYE FTHINGKNLT ETDNLYSVEE 
721:	LIGTTRADKF FGSKFADIFH GADGDDHIEG NDGNDRLYGD KGNDTLSGGN GDDQLYGGDG 
781:	NDKLIGGAGN NYLNGGDGDD ELQVQGNSLA KNVLSGGKGN DKLYGSEGAD LLDGGEGNDL 
841:	LKGGYGNDIY RYLSGYGHHI IDDDGGKDDK LSLADIDFRD VAFRREGNDL IMYKAEGNVL 
901:	SIGHKNGITF KNWFEKESGD ISNHQIEQIF DKDGRVITPD SLKKALEYQQ SNNKASYVYG 
961:	NDALAYGSQG NLNPLINEIS KIISAAGNFD VKEERAAASL LQLSGNASDF SYGRNSITLT 
1021:	ASA