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Protein

Alpha-hemolysin

Gene

hly

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionToxin
Biological processCytolysis, Hemolysis

Enzyme and pathway databases

ReactomeiR-HSA-844456 The NLRP3 inflammasome

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-hemolysin
Short name:
Alpha-HL
Alternative name(s):
Alpha-toxin
Gene namesi
Name:hly
Synonyms:hla
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

ChEMBLiCHEMBL1075259

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000003563627 – 319Alpha-hemolysinAdd BLAST293

Proteomic databases

PRIDEiP09616

Miscellaneous databases

PMAP-CutDBiP09616

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-15848589,EBI-15848589

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-59322N
IntActiP09616, 1 interactor

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP09616
SMRiP09616
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09616

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi145 – 169Gly-richAdd BLAST25

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

Sequence similaritiesi

Belongs to the aerolysin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106UK0 Bacteria
ENOG410YPMH LUCA

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

Sequencei

Sequence statusi: Complete.

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
Checksum:i6711C415DF7EBF30
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01645 Genomic DNA Translation: CAA25801.1
M90536 Genomic DNA Translation: AAA26598.1
PIRiS69209

Similar proteinsi

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:
PDBei
RCSB PDBi
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
PROiPR: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
ProtoNetiSearch...

Entry informationi

Entry nameiHLA_STAAU
AccessioniPrimary (citable) accession number: P09616
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.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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