Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P09616

- HLA_STAAU

UniProt

P09616 - HLA_STAAU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Alpha-hemolysin

Gene

hly

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Heptamer oligomerization and pore formation is required for lytic activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei159 – 1602Cleavage of monomers by proteinase K (minor site)
Sitei161 – 1622Cleavage of monomers by proteinase K (major site)
Sitei164 – 1652Cleavage of monomers by proteinase K (minor site)
Sitei165 – 1662Cleavage of monomers by proteinase K (major site)

GO - Biological processi

  1. hemolysis in other organism Source: UniProtKB-KW
  2. pathogenesis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Toxin

Keywords - Biological processi

Cytolysis, Hemolysis

Enzyme and pathway databases

ReactomeiREACT_75808. The NLRP3 inflammasome.

Protein family/group databases

TCDBi1.C.3.1.1. the -hemolysin channel-forming toxin (hl) 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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

Subcellular locationi

Secreted
Note: Secreted as a monomer. After oligomerization and pore formation, the complex is translocated across the bilayer, probably via the Gly-rich domain of each strand.

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi61 – 611H → L: No oligomerization nor hemolytic activity.
Mutagenesisi61 – 611H → R: No oligomerization nor hemolytic activity.
Mutagenesisi74 – 741H → L: 7% of normal hemolytic activity.
Mutagenesisi170 – 1701H → L: 16% of normal hemolytic activity.
Mutagenesisi285 – 2851H → L: 46% of normal hemolytic activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 319293Alpha-hemolysinPRO_0000035636Add
BLAST

Miscellaneous databases

PMAP-CutDBP09616.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-59322N.

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 314
Turni35 – 384
Beta strandi40 – 434
Beta strandi47 – 559
Turni56 – 594
Beta strandi60 – 6910
Beta strandi74 – 8714
Beta strandi92 – 954
Beta strandi101 – 11515
Beta strandi123 – 1297
Beta strandi135 – 15319
Beta strandi158 – 18427
Beta strandi188 – 19710
Beta strandi200 – 2023
Beta strandi205 – 2084
Turni215 – 2173
Helixi232 – 2343
Helixi239 – 2413
Helixi244 – 2474
Beta strandi254 – 2607
Beta strandi268 – 28619
Beta strandi288 – 31124
Turni312 – 3154
Beta strandi316 – 3183

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
7AHLX-ray1.89A/B/C/D/E/F/G27-319[»]
ProteinModelPortaliP09616.
SMRiP09616. Positions 27-319.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09616.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi145 – 16925Gly-richAdd
BLAST

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.

Sequence similaritiesi

Belongs to the aerolysin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG41533.

Family and domain databases

Gene3Di2.70.240.10. 1 hit.
InterProiIPR005831. Aerolysin/haemolysin_CS.
IPR003963. Bi-component_toxin_staph.
IPR016183. Leukocidin/porin.
[Graphical view]
PfamiPF07968. Leukocidin. 1 hit.
[Graphical view]
PRINTSiPR01468. BICOMPNTOXIN.
SUPFAMiSSF56959. SSF56959. 1 hit.
TIGRFAMsiTIGR01002. hlyII. 1 hit.
PROSITEiPS00274. AEROLYSIN. 1 hit.
[Graphical view]

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:
EMBL
GenBank
DDBJ
Links Updated
X01645 Genomic DNA. Translation: CAA25801.1.
M90536 Genomic DNA. Translation: AAA26598.1.
PIRiS69209.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01645 Genomic DNA. Translation: CAA25801.1 .
M90536 Genomic DNA. Translation: AAA26598.1 .
PIRi S69209.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3M2L X-ray 2.10 A/B/C/D/E/F/G 27-319 [» ]
3M3R X-ray 2.20 A/B/C/D/E/F/G 27-319 [» ]
3M4D X-ray 1.90 A/B/C/D/E/F/G 27-319 [» ]
3M4E X-ray 2.30 A/B/C/D/E/F/G 27-319 [» ]
4IDJ X-ray 3.36 A 27-319 [» ]
7AHL X-ray 1.89 A/B/C/D/E/F/G 27-319 [» ]
ProteinModelPortali P09616.
SMRi P09616. Positions 27-319.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59322N.

Chemistry

ChEMBLi CHEMBL1075259.

Protein family/group databases

TCDBi 1.C.3.1.1. the -hemolysin channel-forming toxin (hl) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG41533.

Enzyme and pathway databases

Reactomei REACT_75808. The NLRP3 inflammasome.

Miscellaneous databases

EvolutionaryTracei P09616.
PMAP-CutDB P09616.
PROi P09616.

Family and domain databases

Gene3Di 2.70.240.10. 1 hit.
InterProi IPR005831. Aerolysin/haemolysin_CS.
IPR003963. Bi-component_toxin_staph.
IPR016183. Leukocidin/porin.
[Graphical view ]
Pfami PF07968. Leukocidin. 1 hit.
[Graphical view ]
PRINTSi PR01468. BICOMPNTOXIN.
SUPFAMi SSF56959. SSF56959. 1 hit.
TIGRFAMsi TIGR01002. hlyII. 1 hit.
PROSITEi PS00274. AEROLYSIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Primary sequence of the alpha-toxin gene from Staphylococcus aureus wood 46."
    Gray G.S., Kehoe M.
    Infect. Immun. 46:615-618(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-44.
    Strain: ATCC 10832 / Wood 46.
  2. Hedengrahn G.
    Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
    Strain: ATCC 10832 / Wood 46.
  3. "Functional expression of the alpha-hemolysin of Staphylococcus aureus in intact Escherichia coli and in cell lysates. Deletion of five C-terminal amino acids selectively impairs hemolytic activity."
    Walker B., Krishnasastry M., Zorn L., Kasianowicz J., Bayley H.
    J. Biol. Chem. 267:10902-10909(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-319, PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 10832 / Wood 46.
  4. "Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore."
    Song L., Hobaugh M.R., Shustak C., Cheley S., Bayley H., Gouaux J.E.
    Science 274:1859-1866(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    Strain: ATCC 10832 / Wood 46.
  5. "Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis."
    Walker B., Krishnasastry M., Zorn L., Bayley H.
    J. Biol. Chem. 267:21782-21786(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  6. "Site-directed mutagenesis of the alpha-toxin gene of Staphylococcus aureus: role of histidines in toxin activity in vitro and in a murine model."
    Menzies B.E., Kernodle D.S.
    Infect. Immun. 62:1843-1847(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HISTIDINE RESIDUES.
  7. "Histidine residues near the N-terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation."
    Jursch R., Hildebrand A., Hobom G., Tranum-Jensen J., Ward R., Kehoe M., Bhakdi S.
    Infect. Immun. 62:2249-2256(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HISTIDINE RESIDUES.
  8. "Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification."
    Walker B., Bayley H.
    J. Biol. Chem. 270:23065-23071(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.

Entry informationi

Entry nameiHLA_STAAU
AccessioniPrimary (citable) accession number: P09616
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 1992
Last modified: October 29, 2014
This is version 108 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

External Data

Dasty 3