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P09616

- HLA_STAAU

UniProt

P09616 - HLA_STAAU

Protein

Alpha-hemolysin

Gene

hly

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (01 Dec 1992)
      Previous versions | rss
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    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

    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-SubCell

    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

    MKTRIVSSVT TTLLLGSILM NPVAGAADSD INIKTGTTDI GSNTTVKTGD    50
    LVTYDKENGM HKKVFYSFID DKNHNKKLLV IRTKGTIAGQ YRVYSEEGAN 100
    KSGLAWPSAF KVQLQLPDNE VAQISDYYPR NSIDTKEYMS TLTYGFNGNV 150
    TGDDTGKIGG LIGANVSIGH TLKYVQPDFK TILESPTDKK VGWKVIFNNM 200
    VNQNWGPYDR DSWNPVYGNQ LFMKTRNGSM KAADNFLDPN KASSLLSSGF 250
    SPDFATVITM DRKASKQQTN IDVIYERVRD DYQLHWTSTN WKGTNTKDKW 300
    TDRSSERYKI DWEKEEMTN 319
    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 1, 2014
    This is version 107 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