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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei155 – 1551Important for oligomerization
Sitei374 – 3741Important for heptamerization
Sitei390 – 3901Important for heptamerization

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi208 – 2081K → A: No effect on heptamerization. 1 Publication
Mutagenesisi211 – 2111D → A: No effect on heptamerization. 1 Publication
Mutagenesisi221 – 2211K → A: Impairs heptamerization. 1 Publication
Mutagenesisi244 – 2441Y → 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 Publication
Mutagenesisi305 – 3051R → A: Impairs heptamerization. 1 Publication
Mutagenesisi313 – 3131K → A: No effect on heptamerization. 1 Publication
Mutagenesisi330 – 3301E → A: No effect on heptamerization. 1 Publication
Mutagenesisi332 – 3321K → A: No effect on heptamerization. 1 Publication
Mutagenesisi374 – 3741K → A: Impairs heptamerization. 1 Publication
Mutagenesisi390 – 3901E → A: Nearly abolishes heptamerization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 445422AerolysinPRO_0000035620Add
BLAST
Propeptidei446 – 49348PRO_0000035621Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

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 interactions.
MINTiMINT-1958193.
STRINGi380703.AHA_0438.

Structurei

Secondary structure

1
493
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 313Combined sources
Beta strandi33 – 353Combined sources
Beta strandi46 – 483Combined sources
Helixi51 – 566Combined sources
Helixi58 – 625Combined sources
Beta strandi70 – 723Combined sources
Turni74 – 763Combined sources
Beta strandi77 – 804Combined sources
Helixi82 – 843Combined sources
Beta strandi88 – 903Combined sources
Beta strandi94 – 1029Combined sources
Beta strandi114 – 1163Combined sources
Helixi121 – 1299Combined sources
Turni132 – 1354Combined sources
Helixi136 – 14510Combined sources
Beta strandi162 – 1687Combined sources
Beta strandi171 – 1766Combined sources
Turni185 – 1884Combined sources
Beta strandi192 – 20211Combined sources
Helixi204 – 2063Combined sources
Beta strandi213 – 22917Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi237 – 25216Combined sources
Helixi257 – 2604Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi284 – 2863Combined sources
Helixi288 – 2903Combined sources
Beta strandi293 – 30412Combined sources
Beta strandi312 – 34534Combined sources
Beta strandi352 – 3543Combined sources
Beta strandi361 – 37010Combined sources
Helixi374 – 3763Combined sources
Helixi378 – 3847Combined sources
Helixi388 – 3903Combined sources
Beta strandi392 – 3943Combined sources
Helixi396 – 4038Combined sources
Helixi405 – 41511Combined sources
Beta strandi419 – 43416Combined sources
Beta strandi465 – 4673Combined sources
Helixi472 – 4776Combined sources
Beta strandi481 – 4899Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP09167.
SMRiP09167. Positions 25-491.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09167.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 8417Interaction with host N-linked glycanAdd
BLAST
Regioni256 – 28833Part of the transmembrane beta-barrel after proteolytic activation of the toxin and insertion into the host membraneAdd
BLAST
Regioni346 – 35510Interaction with glycans from host GPI-anchor

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. C-type_lectin_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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti277 – 2771E → Q in AAA21938 (PubMed:3584074).Curated
Sequence conflicti283 – 2831A → R in AAA21938 (PubMed:3584074).Curated
Sequence conflicti472 – 4721A → R in AAA21938 (PubMed:3584074).Curated

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
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[»]
ProteinModelPortaliP09167.
SMRiP09167. Positions 25-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

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

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. C-type_lectin_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: March 16, 2016
This is version 109 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.