ID   HLGC_STAAS              Reviewed;         315 AA.
AC   Q6G6Q1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Gamma-hemolysin component C;
DE   Flags: Precursor;
GN   Name=hlgC; OrderedLocusNames=SAS2311;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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. HlgC (class S) associates with HlgB (class
CC       F) thus forming an CB toxin (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
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DR   EMBL; BX571857; CAG44124.1; -; Genomic_DNA.
DR   RefSeq; WP_000916709.1; NC_002953.3.
DR   AlphaFoldDB; Q6G6Q1; -.
DR   SMR; Q6G6Q1; -.
DR   KEGG; sas:SAS2311; -.
DR   HOGENOM; CLU_075311_0_0_9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; Signal; Toxin; Virulence.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..315
FT                   /note="Gamma-hemolysin component C"
FT                   /id="PRO_0000045224"
SQ   SEQUENCE   315 AA;  35598 MW;  DF04C573DFAD2DDF CRC64;
     MLKNKILATT LSVSLLAPLA NPLLENAKAA NDTEEIGKGS DIEIIKRTED KTSNKWGVTQ
     NIQFDFVKDK KYNKDALILK MQGFISSRTT YYNYKKTNHV KAMRWPFQYN IGLKTNDKYV
     SLINYLPKNK IESTNVSQTL GYNIGGNFQS APSLGGNGSF NYSKSISYTQ QNYVSEVEQQ
     NSKSVLWGVK ANSFATESGQ KSAFDSDLFV GYKPHSKDPR DYFVPDSELP PLVQSGFNPS
     FIATVSHEKG SSDTSEFEIT YGRNMDVTHA IKRSTHYGNS YLDGHRVHNA FVNRNYTVKY
     EVNWKTHEIK VKGQN