ID   HLGA_STAAR              Reviewed;         309 AA.
AC   Q6GE14;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Gamma-hemolysin component A;
DE   AltName: Full=H-gamma-2;
DE   AltName: Full=H-gamma-II;
DE   Flags: Precursor;
GN   Name=hlgA; OrderedLocusNames=SAR2509;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Toxin that seems to act by forming pores in the membrane of
CC       the cell. Has a hemolytic and a leucotoxic activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Toxicity requires sequential binding and synergistic
CC       association of a class S and a class F component which form
CC       heterooligomeric complexes. HlgA (class S) associates with HlgB (class
CC       F) thus forming an AB toxin in strains producing both gamma-hemolysins
CC       and leukocidins. HlgA and LukF-PV can also form a complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX571856; CAG41489.1; -; Genomic_DNA.
DR   RefSeq; WP_000594517.1; NC_002952.2.
DR   AlphaFoldDB; Q6GE14; -.
DR   SMR; Q6GE14; -.
DR   KEGG; sar:SAR2509; -.
DR   HOGENOM; CLU_075311_0_0_9; -.
DR   OMA; ANPFTEI; -.
DR   OrthoDB; 692853at2; -.
DR   Proteomes; UP000000596; 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; 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.
PE   3: Inferred from homology;
KW   Cytolysis; Hemolysis; Secreted; Signal; Toxin; Virulence.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000250"
FT   CHAIN           30..309
FT                   /note="Gamma-hemolysin component A"
FT                   /id="PRO_0000045215"
SQ   SEQUENCE   309 AA;  34958 MW;  184AF6092034B60F CRC64;
     MIKNKILTAT LAVGLIAPLA NPFIEISKAE NKIEDIGQGA EIIKRTQDIT SKRLAITQNI
     QFDFVKDKKY NKDALVVKMQ GFISSRTTYS DLKKYPYIKR MIWPFQYNIS LKTKDSNVDL
     INYLPKNKID SADVSQKLGY NIGGNFQSAP SIGGSGSFNY SKTISYNQKN YVTEVESQNS
     KGVKWGVKAN SFVTPNGQVS AYDQYLFAQD PTGPAARDYF VPDNQLPPLI QSGFNPSFIT
     TLSHEKGKGD KSEFEITYGR NMDTTYAYVT RHRLAVDRKH DAFKNRNVTV KYEVNWKTHE
     VKIKSITPK