AERA_AEREN
ID AERA_AEREN Reviewed; 492 AA.
AC P09166;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Aerolysin;
DE Flags: Precursor;
GN Name=aerA;
OS Aeromonas enteropelogenes (Aeromonas trota).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=29489;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=AB3;
RX PubMed=2459581; DOI=10.1111/j.1365-2958.1988.tb00057.x;
RA Husslein V., Huhle B., Jarchau T., Lurz R., Goebel W., Chakraborty T.;
RT "Nucleotide sequence and transcriptional analysis of the aerCaerA region of
RT Aeromonas sobria encoding aerolysin and its regulatory region.";
RL Mol. Microbiol. 2:507-517(1988).
CC -!- FUNCTION: Secreted, cytolytic toxin that forms pores in host membranes
CC after proteolytic removal of a C-terminal propeptide, leading to
CC destruction of the membrane permeability barrier and cell death. The
CC pores are formed by transmembrane beta-strands and are approximately 3
CC nm in diameter (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer in solution; homoheptamer in the host membrane.
CC After binding to GPI-anchored proteins in target membranes and
CC proteolytic removal of the C-terminal propeptide, the protein assembles
CC into a heptameric pre-pore complex. A further conformation change leads
CC to insertion into the host membrane (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2459581}. Host cell
CC membrane {ECO:0000269|PubMed:2459581}. Note=Secreted as a soluble
CC precursor.
CC -!- DOMAIN: The C-terminal propeptide is required for normal protein
CC folding and secretion; it maintains the aerolysin precursor in its
CC soluble form and prevents premature heptamerization and pore formation.
CC {ECO:0000250}.
CC -!- PTM: Proteolytic cleavage and subsequent release of the propeptide
CC trigger a major conformation change, leading to the formation of a
CC heptameric pre-pore that then inserts into the host membrane.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from A.sobria.
CC {ECO:0000305}.
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DR EMBL; Y00559; CAA68642.1; -; Genomic_DNA.
DR RefSeq; WP_042070784.1; NZ_CDDE01000012.1.
DR AlphaFoldDB; P09166; -.
DR SMR; P09166; -.
DR OrthoDB; 585450at2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.10.40.10; -; 1.
DR InterPro; IPR005831; Aerolysin/haemolysin_CS.
DR InterPro; IPR005830; Aerolysn.
DR InterPro; IPR005138; APT_dom.
DR InterPro; IPR037015; APT_N_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF01117; Aerolysin; 1.
DR Pfam; PF03440; APT; 1.
DR PRINTS; PR00754; AEROLYSIN.
DR SMART; SM00999; Aerolysin; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00274; AEROLYSIN; 1.
PE 3: Inferred from homology;
KW Cytolysis; Disulfide bond; Hemolysis; Host cell membrane; Host membrane;
KW Membrane; Secreted; Signal; Toxin; Transmembrane;
KW Transmembrane beta strand; Virulence.
FT SIGNAL 1..21
FT CHAIN 22..445
FT /note="Aerolysin"
FT /id="PRO_0000035632"
FT PROPEP 446..492
FT /id="PRO_0000035633"
FT REGION 68..84
FT /note="Interaction with host N-linked glycan"
FT /evidence="ECO:0000250"
FT REGION 256..288
FT /note="Part of the transmembrane beta-barrel after
FT proteolytic activation of the toxin and insertion into the
FT host membrane"
FT /evidence="ECO:0000250"
FT REGION 346..355
FT /note="Interaction with glycans from host GPI-anchor"
FT /evidence="ECO:0000250"
FT SITE 155
FT /note="Important for oligomerization"
FT /evidence="ECO:0000250"
FT SITE 374
FT /note="Important for heptamerization"
FT /evidence="ECO:0000250"
FT SITE 390
FT /note="Important for heptamerization"
FT /evidence="ECO:0000250"
FT DISULFID 42..98
FT /evidence="ECO:0000250"
FT DISULFID 182..187
FT /evidence="ECO:0000250"
SQ SEQUENCE 492 AA; 54493 MW; 520F25D2B6CA9A38 CRC64;
MKALKITGLS LIISATLAAQ TNAAEPIYPD QLRLFSLGED VCGTDYRPIN REEAQSVRNN
IVAMMGQWQI SGLANNWVIL GPGYNGEIKP GKASTTWCYP TRPATAEIPV LPAFNIPDGD
AVDVQWRMVH DSANFIKPVS YLAHYLGYAW VGGDHSQFVG DDMDVIQEGD DWVLRGNDGG
KCDGYRCNEK SSIRVSNFAY TLDPGSFSHG DVTQSERTLV HTVVGWATNI SDTPQSGYDV
TLNYTTMSNW SKTNTYGLSE KVSTKNKFKW PLVGETEVSI EIAANQSWAS QNGGAVTTAL
SQSVRPVVPA RSRVPVKIEL YKANISYPYE FKADMSYDLT FNGFLRWGGN AWHTHPEDRP
TLSHTFAIGP FKDKASSIRY QWDKRYLPGE MKWWDWNWAI QQNGLATMQD SLARVLRPVR
ASITGDFRAE SQFAGNIEIG TPVPLGSDSK VRRTRSVDGA NTGLKLDIPL DAQELAELGF
ENVTLSVTPA RN