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Entry version 123 (16 Oct 2019)
Sequence version 2 (01 Dec 1992)
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Protein

Aerolysin

Gene

aerA

Organism
Aeromonas hydrophila
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei155Important for oligomerization1
Sitei374Important for heptamerization1
Sitei390Important for heptamerization1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionToxin
Biological processVirulence

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.C.4.1.1 the aerolysin channel-forming toxin (aerolysin) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Aerolysin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:aerA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAeromonas hydrophila
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri644 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23Add BLAST23
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003562024 – 445AerolysinAdd BLAST422
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000035621446 – 493Add BLAST48

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi42 ↔ 98
Disulfide bondi182 ↔ 187

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P09167

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-8027669,EBI-8027669

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-42724N

Protein interaction database and analysis system

More...
IntActi
P09167, 2 interactors

Molecular INTeraction database

More...
MINTi
P09167

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1493
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P09167

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P09167

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the aerolysin family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4107Y8H Bacteria
ENOG410ZHRV LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005831 Aerolysin/haemolysin_CS
IPR005830 Aerolysn
IPR005138 APT_dom
IPR037015 APT_N_sf
IPR016187 CTDL_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01117 Aerolysin, 1 hit
PF03440 APT, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00754 AEROLYSIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00999 Aerolysin, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56436 SSF56436, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00274 AEROLYSIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD396CE4EAD85AEF0
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M16495 Genomic DNA Translation: AAA21938.1 Frameshift.
M29818 Genomic DNA Translation: AAA21934.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A25976

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
SMRiP09167
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-42724N
IntActiP09167, 2 interactors
MINTiP09167

Protein family/group databases

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

Phylogenomic databases

eggNOGiENOG4107Y8H Bacteria
ENOG410ZHRV LUCA

Miscellaneous databases

EvolutionaryTraceiP09167
PMAP-CutDBiP09167

Family and domain databases

Gene3Di3.10.40.10, 1 hit
InterProiView protein in InterPro
IPR005831 Aerolysin/haemolysin_CS
IPR005830 Aerolysn
IPR005138 APT_dom
IPR037015 APT_N_sf
IPR016187 CTDL_fold
PfamiView protein in Pfam
PF01117 Aerolysin, 1 hit
PF03440 APT, 1 hit
PRINTSiPR00754 AEROLYSIN
SMARTiView protein in SMART
SM00999 Aerolysin, 1 hit
SUPFAMiSSF56436 SSF56436, 1 hit
PROSITEiView protein in PROSITE
PS00274 AEROLYSIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAERA_AERHY
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P09167
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 1992
Last modified: October 16, 2019
This is version 123 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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