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Protein

Aerolysin

Gene

aerA

Organism
Aeromonas hydrophila
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and host cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei155Important for oligomerization1
Sitei374Important for heptamerization1
Sitei390Important for heptamerization1

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Toxin

Protein family/group databases

TCDBi1.C.4.1.1. the aerolysin channel-forming toxin (aerolysin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Aerolysin
Gene namesi
Name:aerA
OrganismiAeromonas hydrophila
Taxonomic identifieri644 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi208K → A: No effect on heptamerization. 1 Publication1
Mutagenesisi211D → A: No effect on heptamerization. 1 Publication1
Mutagenesisi221K → A: Impairs heptamerization. 1 Publication1
Mutagenesisi244Y → G: Blocks the hemolytic activity. Does not affect the initial structure, the ability to bind to cell-surface receptors or the capacity to form heptamers. Does not insert into membranes and form pores; the mutant heptamer is hydrophilic instead of being hydrophobic. 1 Publication1
Mutagenesisi305R → A: Impairs heptamerization. 1 Publication1
Mutagenesisi313K → A: No effect on heptamerization. 1 Publication1
Mutagenesisi330E → A: No effect on heptamerization. 1 Publication1
Mutagenesisi332K → A: No effect on heptamerization. 1 Publication1
Mutagenesisi374K → A: Impairs heptamerization. 1 Publication1
Mutagenesisi390E → A: Nearly abolishes heptamerization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Add BLAST23
ChainiPRO_000003562024 – 445AerolysinAdd BLAST422
PropeptideiPRO_0000035621446 – 493Add BLAST48

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi42 ↔ 98
Disulfide bondi182 ↔ 187

Post-translational modificationi

Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane.

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP09167.

Miscellaneous databases

PMAP-CutDBP09167.

Interactioni

Subunit structurei

Homodimer in solution; homoheptamer in the host membrane. After binding to GPI-anchored proteins in target membranes and proteolytic removal of the C-terminal propeptide, the protein assembles into a heptameric pre-pore complex. A further conformation change leads to insertion into the host membrane.4 Publications

Protein-protein interaction databases

DIPiDIP-42724N.
IntActiP09167. 2 interactors.
MINTiMINT-1958193.
STRINGi380703.AHA_0438.

Structurei

Secondary structure

1493
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 31Combined sources3
Beta strandi33 – 35Combined sources3
Beta strandi46 – 48Combined sources3
Helixi51 – 56Combined sources6
Helixi58 – 62Combined sources5
Beta strandi70 – 72Combined sources3
Turni74 – 76Combined sources3
Beta strandi77 – 80Combined sources4
Helixi82 – 84Combined sources3
Beta strandi88 – 90Combined sources3
Beta strandi94 – 102Combined sources9
Beta strandi114 – 116Combined sources3
Helixi121 – 129Combined sources9
Turni132 – 135Combined sources4
Helixi136 – 145Combined sources10
Beta strandi162 – 168Combined sources7
Beta strandi171 – 176Combined sources6
Turni185 – 188Combined sources4
Beta strandi192 – 202Combined sources11
Helixi204 – 206Combined sources3
Beta strandi213 – 229Combined sources17
Beta strandi231 – 233Combined sources3
Beta strandi237 – 252Combined sources16
Helixi257 – 260Combined sources4
Beta strandi274 – 276Combined sources3
Beta strandi284 – 286Combined sources3
Helixi288 – 290Combined sources3
Beta strandi293 – 304Combined sources12
Beta strandi312 – 345Combined sources34
Beta strandi352 – 354Combined sources3
Beta strandi361 – 370Combined sources10
Helixi374 – 376Combined sources3
Helixi378 – 384Combined sources7
Helixi388 – 390Combined sources3
Beta strandi392 – 394Combined sources3
Helixi396 – 403Combined sources8
Helixi405 – 415Combined sources11
Beta strandi419 – 434Combined sources16
Beta strandi465 – 467Combined sources3
Helixi472 – 477Combined sources6
Beta strandi481 – 489Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PREX-ray2.80A/B24-493[»]
1Z52X-ray2.38A/B24-493[»]
3C0MX-ray2.88A/B24-493[»]
3C0NX-ray2.20A/B24-493[»]
3C0OX-ray2.50A/B24-493[»]
3G4NX-ray2.10A/B24-493[»]
3G4OX-ray2.30A/B24-493[»]
5JZHelectron microscopy3.90A/B/C/D/E/F/G/H/I/J/K/L/M/N24-447[»]
5JZTelectron microscopy7.40A/B/C/D/E/F/G24-447[»]
5JZWelectron microscopy4.46A/B/C/D/E/F/G/H/I/J/K/L/M/N24-447[»]
ProteinModelPortaliP09167.
SMRiP09167.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09167.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni68 – 84Interaction with host N-linked glycanAdd BLAST17
Regioni256 – 288Part of the transmembrane beta-barrel after proteolytic activation of the toxin and insertion into the host membraneAdd BLAST33
Regioni346 – 355Interaction with glycans from host GPI-anchor10

Domaini

The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation.1 Publication

Sequence similaritiesi

Belongs to the aerolysin family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4107Y8H. Bacteria.
ENOG410ZHRV. LUCA.

Family and domain databases

Gene3Di2.170.15.10. 1 hit.
3.10.40.10. 1 hit.
InterProiIPR023307. Aerolysin-like_beta_cmplx_dom.
IPR005831. Aerolysin/haemolysin_CS.
IPR005830. Aerolysn.
IPR005138. APT.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF01117. Aerolysin. 1 hit.
PF03440. APT. 1 hit.
[Graphical view]
PRINTSiPR00754. AEROLYSIN.
SMARTiSM00999. Aerolysin. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00274. AEROLYSIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09167-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKIKLTGLS LIISGLLMAQ AQAAEPVYPD QLRLFSLGQG VCGDKYRPVN
60 70 80 90 100
REEAQSVKSN IVGMMGQWQI SGLANGWVIM GPGYNGEIKP GTASNTWCYP
110 120 130 140 150
TNPVTGEIPT LSALDIPDGD EVDVQWRLVH DSANFIKPTS YLAHYLGYAW
160 170 180 190 200
VGGNHSQYVG EDMDVTRDGD GWVIRGNNDG GCDGYRCGDK TAIKVSNFAY
210 220 230 240 250
NLDPDSFKHG DVTQSDRQLV KTVVGWAVND SDTPQSGYDV TLRYDTATNW
260 270 280 290 300
SKTNTYGLSE KVTTKNKFKW PLVGETELSI EIAANQSWAS QNGGSTTTSL
310 320 330 340 350
SQSVRPTVPA RSKIPVKIEL YKADISYPYE FKADVSYDLT LSGFLRWGGN
360 370 380 390 400
AWYTHPDNRP NWNHTFVIGP YKDKASSIRY QWDKRYIPGE VKWWDWNWTI
410 420 430 440 450
QQNGLSTMQN NLARVLRPVR AGITGDFSAE SQFAGNIEIG APVPLAADSK
460 470 480 490
VRRARSVDGA GQGLRLEIPL DAQELSGLGF NNVSLSVTPA ANQ
Length:493
Mass (Da):54,342
Last modified:December 1, 1992 - v2
Checksum:iD396CE4EAD85AEF0
GO

Sequence cautioni

The sequence AAA21938 differs from that shown. Reason: Frameshift at position 483.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti277E → Q in AAA21938 (PubMed:3584074).Curated1
Sequence conflicti283A → R in AAA21938 (PubMed:3584074).Curated1
Sequence conflicti472A → R in AAA21938 (PubMed:3584074).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16495 Genomic DNA. Translation: AAA21938.1. Frameshift.
M29818 Genomic DNA. Translation: AAA21934.1.
PIRiA25976.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16495 Genomic DNA. Translation: AAA21938.1. Frameshift.
M29818 Genomic DNA. Translation: AAA21934.1.
PIRiA25976.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PREX-ray2.80A/B24-493[»]
1Z52X-ray2.38A/B24-493[»]
3C0MX-ray2.88A/B24-493[»]
3C0NX-ray2.20A/B24-493[»]
3C0OX-ray2.50A/B24-493[»]
3G4NX-ray2.10A/B24-493[»]
3G4OX-ray2.30A/B24-493[»]
5JZHelectron microscopy3.90A/B/C/D/E/F/G/H/I/J/K/L/M/N24-447[»]
5JZTelectron microscopy7.40A/B/C/D/E/F/G24-447[»]
5JZWelectron microscopy4.46A/B/C/D/E/F/G/H/I/J/K/L/M/N24-447[»]
ProteinModelPortaliP09167.
SMRiP09167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42724N.
IntActiP09167. 2 interactors.
MINTiMINT-1958193.
STRINGi380703.AHA_0438.

Protein family/group databases

TCDBi1.C.4.1.1. the aerolysin channel-forming toxin (aerolysin) family.

Proteomic databases

PRIDEiP09167.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107Y8H. Bacteria.
ENOG410ZHRV. LUCA.

Miscellaneous databases

EvolutionaryTraceiP09167.
PMAP-CutDBP09167.

Family and domain databases

Gene3Di2.170.15.10. 1 hit.
3.10.40.10. 1 hit.
InterProiIPR023307. Aerolysin-like_beta_cmplx_dom.
IPR005831. Aerolysin/haemolysin_CS.
IPR005830. Aerolysn.
IPR005138. APT.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF01117. Aerolysin. 1 hit.
PF03440. APT. 1 hit.
[Graphical view]
PRINTSiPR00754. AEROLYSIN.
SMARTiSM00999. Aerolysin. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00274. AEROLYSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAERA_AERHY
AccessioniPrimary (citable) accession number: P09167
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 1992
Last modified: November 30, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.