HLA_STAA8
ID HLA_STAA8 Reviewed; 319 AA.
AC Q2G1X0;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Alpha-hemolysin;
DE Short=Alpha-HL;
DE AltName: Full=Alpha-toxin;
DE Flags: Precursor;
GN Name=hly; Synonyms=hla; OrderedLocusNames=SAOUHSC_01121;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=8325-4;
RX PubMed=3679545; DOI=10.1128/iai.55.12.3103-3110.1987;
RA Patel A.H., Nowlan P., Weavers E.D., Foster T.;
RT "Virulence of protein A-deficient and alpha-toxin-deficient mutants of
RT Staphylococcus aureus isolated by allele replacement.";
RL Infect. Immun. 55:3103-3110(1987).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=RN4220;
RX PubMed=20472795; DOI=10.1128/jb.01452-09;
RA Sibbald M.J., Winter T., van der Kooi-Pol M.M., Buist G., Tsompanidou E.,
RA Bosma T., Schafer T., Ohlsen K., Hecker M., Antelmann H., Engelmann S.,
RA van Dijl J.M.;
RT "Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in
RT Staphylococcus aureus.";
RL J. Bacteriol. 192:3788-3800(2010).
CC -!- FUNCTION: Alpha-toxin binds to the membrane of eukaryotic cells
CC resulting in the release of low-molecular weight molecules and leading
CC to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to
CC the lesion region (Probable). Heptamer oligomerization and pore
CC formation is required for lytic activity (By similarity).
CC {ECO:0000250|UniProtKB:P09616, ECO:0000305|PubMed:3679545}.
CC -!- SUBUNIT: Self-assembles to form first a non-lytic oligomeric
CC intermediate and then, a mushroom-shaped homoheptamer structure of 100
CC Angstroms in length and up to 100 Angstroms in diameter.
CC {ECO:0000250|UniProtKB:P09616}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20472795}.
CC Note=Secreted as a monomer. After oligomerization and pore formation,
CC the complex is translocated across the bilayer, probably via the Gly-
CC rich domain of each strand. {ECO:0000250|UniProtKB:P09616}.
CC -!- INDUCTION: Less protein is secreted in a secG or double secG/secY2
CC mutant (at protein level). {ECO:0000269|PubMed:20472795}.
CC -!- DOMAIN: The mushroom-shaped heptamer is composed of a cap domain
CC (comprising 7 beta sandwiches and the amino latches of each protomer),
CC 7 rim regions whose protruding strands may interact with the membrane
CC bilayer, and the stem domain (52 Angstroms in length, 26 Angstroms in
CC diameter) which forms the transmembrane pore.
CC {ECO:0000250|UniProtKB:P09616}.
CC -!- DISRUPTION PHENOTYPE: About 10-fold decrease in virulence in mice,
CC increased presence of neutrophils in the injection region.
CC {ECO:0000269|PubMed:3679545}.
CC -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
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DR EMBL; CP000253; ABD30233.1; -; Genomic_DNA.
DR RefSeq; WP_000857483.1; NZ_LS483365.1.
DR RefSeq; YP_499665.1; NC_007795.1.
DR PDB; 4U6V; X-ray; 2.56 A; A/B=27-319.
DR PDBsum; 4U6V; -.
DR AlphaFoldDB; Q2G1X0; -.
DR SMR; Q2G1X0; -.
DR STRING; 1280.SAXN108_1158; -.
DR ABCD; Q2G1X0; 20 sequenced antibodies.
DR EnsemblBacteria; ABD30233; ABD30233; SAOUHSC_01121.
DR GeneID; 3920722; -.
DR KEGG; sao:SAOUHSC_01121; -.
DR PATRIC; fig|93061.5.peg.1029; -.
DR eggNOG; ENOG50348U0; Bacteria.
DR HOGENOM; CLU_055394_0_1_9; -.
DR OMA; KWPSAYH; -.
DR PRO; PR:Q2G1X0; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR005831; Aerolysin/haemolysin_CS.
DR InterPro; IPR003963; Bi-component_toxin_staph.
DR InterPro; IPR016183; Leukocidin/Hemolysin_toxin.
DR InterPro; IPR036435; Leukocidin/porin_MspA_sf.
DR Pfam; PF07968; Leukocidin; 1.
DR PRINTS; PR01468; BICOMPNTOXIN.
DR SUPFAM; SSF56959; SSF56959; 1.
DR TIGRFAMs; TIGR01002; hlyII; 1.
DR PROSITE; PS00274; AEROLYSIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Hemolysis; Reference proteome; Secreted; Signal;
KW Toxin; Virulence.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..319
FT /note="Alpha-hemolysin"
FT /id="PRO_0000414600"
FT STRAND 44..55
FT /evidence="ECO:0007829|PDB:4U6V"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 60..71
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 74..88
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 101..115
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:4U6V"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:4U6V"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:4U6V"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:4U6V"
FT TURN 244..248
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 254..263
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 268..286
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 288..311
FT /evidence="ECO:0007829|PDB:4U6V"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:4U6V"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:4U6V"
SQ SEQUENCE 319 AA; 35973 MW; DAA5DCE482CC4C33 CRC64;
MKTRIVSSVT TTLLLGSILM NPVANAADSD INIKTGTTDI GSNTTVKTGD LVTYDKENGM
HKKVFYSFID DKNHNKKLLV IRTKGTIAGQ YRVYSEEGAN KSGLAWPSAF KVQLQLPDNE
VAQISDYYPR NSIDTKEYMS TLTYGFNGNV TGDDTGKIGG LIGANVSIGH TLKYVQPDFK
TILESPTDKK VGWKVIFNNM VNQNWGPYDR DSWNPVYGNQ LFMKTRNGSM KAADNFLDPN
KASSLLSSGF SPDFATVITM DRKASKQQTN IDVIYERVRD DYQLHWTSTN WKGTNTKDKW
IDRSSERYKI DWEKEEMTN
