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Protein

Alpha-hemolysin

Gene

hly

Organism
Staphylococcus aureus
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

Alpha-toxin binds to the membrane of eukaryotic cells (particularly red blood cells, RBC) forming pores, resulting in hemolysis, with the release of low-molecular weight molecules leading to eventual osmotic RBC lysis. Human RBCs bind much less alpha-toxin than do rabbit RBCs (PubMed:1587866). Heptamer oligomerization and pore formation is required for lytic activity.1 Publication

<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

  • identical protein binding Source: IntAct
  • toxin activity Source: UniProtKB-KW

GO - Biological processi

<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 processCytolysis, Hemolysis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-844456 The NLRP3 inflammasome

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.C.3.1.1 the Alpha-hemolysin channel-forming toxin (Alphahl) 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:
Alpha-hemolysin
Short name:
Alpha-HL
Alternative name(s):
Alpha-toxin
<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:hly
Synonyms:hla
<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>OrganismiStaphylococcus aureus
<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 identifieri1280 [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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

<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

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>Mutagenesisi28 – 65Missing : Binds host red blood cells, complete loss of hemolytic activity, no longer oligomerizes. 1 PublicationAdd BLAST38
Mutagenesisi28 – 49Missing : Binds host red blood cells, complete loss of hemolytic activity, forms hexamers. 1 PublicationAdd BLAST22
Mutagenesisi28 – 39Missing : Binds host red blood cells, complete loss of hemolytic activity, mainly forms pentamers. 1 PublicationAdd BLAST12
Mutagenesisi28 – 29Missing : Binds host red blood cells, complete loss of hemolytic activity, mainly forms pentamers. 1 Publication2
Mutagenesisi61H → I, L, P, R, S or T: No oligomerization nor hemolytic activity, wild-type target cell-binding. 1 Publication1
Mutagenesisi61H → L: No hemolytic activity, reduced oligomerization, not toxic in mice. 1 Publication1
Mutagenesisi74H → I, R or T: No oligomerization, altered hemolysis, near wild-type target cell binding. 1 Publication1
Mutagenesisi74H → L: 7% of normal hemolytic activity, reduced toxicity in mice. 1 Publication1
Mutagenesisi170H → L, P or R: Decreased hemolysis, wild-type oligomerization and target cell binding. 1 Publication1
Mutagenesisi170H → L: 16% of normal hemolytic activity. 1 Publication1
Mutagenesisi285H → I, P, R or S: Nearly wild-type oligomerization, hemolysis and target cell binding. 1 Publication1
Mutagenesisi285H → L: 46% of normal hemolytic activity, slowly toxic in mice. 1 Publication1
Mutagenesisi312 – 319Missing : Binds host red blood cells, complete loss of hemolytic activity, no longer oligomerizes. 1 Publication8
Mutagenesisi315 – 319Missing : Binds host red blood cells, almost complete loss of hemolytic activity, greatly reduced oligomerization. 2 Publications5
Mutagenesisi317 – 319Missing : Binds host red blood cells, almost complete loss of hemolytic activity, greatly reduced oligomerization. 1 Publication3

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075259

<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 – 261 PublicationAdd BLAST26
<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_000003563627 – 319Alpha-hemolysinAdd BLAST293

Proteomic databases

PRoteomics IDEntifications database

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PRIDEi
P09616

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P09616

<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

Self-assembles to first form a non-lytic oligomeric intermediate, and then, a mushroom-shaped homoheptamer structure of 100 Angstroms in length and up to 100 Angstroms in diameter.2 Publications1 Publication

<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
itself6EBI-15848589,EBI-15848589

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-59322N

Protein interaction database and analysis system

More...
IntActi
P09616, 1 interactor

<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

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P09616

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

More...
SMRi
P09616

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P09616

<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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi145 – 169Gly-richAdd BLAST25

<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 mushroom-shaped heptamer is composed of a cap domain (comprising 7 beta sandwiches and the amino latches of each protomer), 7 rim regions whose protruding strands may interact with the membrane bilayer, and the stem domain (52 Angstroms in length, 26 Angstroms in diameter) which forms the transmembrane pore.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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4106UK0 Bacteria
ENOG410YPMH LUCA

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005831 Aerolysin/haemolysin_CS
IPR003963 Bi-component_toxin_staph
IPR016183 Leukocidin/Hemolysin_toxin
IPR036435 Leukocidin/porin_MspA_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07968 Leukocidin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01468 BICOMPNTOXIN

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56959 SSF56959, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01002 hlyII, 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>.<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.

P09616-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKTRIVSSVT TTLLLGSILM NPVAGAADSD INIKTGTTDI GSNTTVKTGD
60 70 80 90 100
LVTYDKENGM HKKVFYSFID DKNHNKKLLV IRTKGTIAGQ YRVYSEEGAN
110 120 130 140 150
KSGLAWPSAF KVQLQLPDNE VAQISDYYPR NSIDTKEYMS TLTYGFNGNV
160 170 180 190 200
TGDDTGKIGG LIGANVSIGH TLKYVQPDFK TILESPTDKK VGWKVIFNNM
210 220 230 240 250
VNQNWGPYDR DSWNPVYGNQ LFMKTRNGSM KAADNFLDPN KASSLLSSGF
260 270 280 290 300
SPDFATVITM DRKASKQQTN IDVIYERVRD DYQLHWTSTN WKGTNTKDKW
310
TDRSSERYKI DWEKEEMTN
Length:319
Mass (Da):35,904
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:i6711C415DF7EBF30
GO

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
X01645 Genomic DNA Translation: CAA25801.1
M90536 Genomic DNA Translation: AAA26598.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S69209

<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
X01645 Genomic DNA Translation: CAA25801.1
M90536 Genomic DNA Translation: AAA26598.1
PIRiS69209

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
3M2LX-ray2.10A/B/C/D/E/F/G27-319[»]
3M3RX-ray2.20A/B/C/D/E/F/G27-319[»]
3M4DX-ray1.90A/B/C/D/E/F/G27-319[»]
3M4EX-ray2.30A/B/C/D/E/F/G27-319[»]
4IDJX-ray3.36A27-319[»]
4YHDX-ray2.80A/B/C/D/E/G27-319[»]
7AHLX-ray1.89A/B/C/D/E/F/G27-319[»]
ProteinModelPortaliP09616
SMRiP09616
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59322N
IntActiP09616, 1 interactor

Chemistry databases

ChEMBLiCHEMBL1075259

Protein family/group databases

TCDBi1.C.3.1.1 the Alpha-hemolysin channel-forming toxin (Alphahl) family

Proteomic databases

PRIDEiP09616

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4106UK0 Bacteria
ENOG410YPMH LUCA

Enzyme and pathway databases

ReactomeiR-HSA-844456 The NLRP3 inflammasome

Miscellaneous databases

EvolutionaryTraceiP09616
PMAP-CutDBiP09616

Protein Ontology

More...
PROi
PR:P09616

Family and domain databases

InterProiView protein in InterPro
IPR005831 Aerolysin/haemolysin_CS
IPR003963 Bi-component_toxin_staph
IPR016183 Leukocidin/Hemolysin_toxin
IPR036435 Leukocidin/porin_MspA_sf
PfamiView protein in Pfam
PF07968 Leukocidin, 1 hit
PRINTSiPR01468 BICOMPNTOXIN
SUPFAMiSSF56959 SSF56959, 1 hit
TIGRFAMsiTIGR01002 hlyII, 1 hit
PROSITEiView protein in PROSITE
PS00274 AEROLYSIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiHLA_STAAU
<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: P09616
<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 10, 2018
This is version 130 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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