ID   HLGC_STAAR              Reviewed;         315 AA.
AC   Q6GE13;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Gamma-hemolysin component C;
DE   Flags: Precursor;
GN   Name=hlgC; OrderedLocusNames=SAR2510;
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. 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; BX571856; CAG41490.1; -; Genomic_DNA.
DR   RefSeq; WP_000916697.1; NC_002952.2.
DR   AlphaFoldDB; Q6GE13; -.
DR   SMR; Q6GE13; -.
DR   KEGG; sar:SAR2510; -.
DR   HOGENOM; CLU_075311_0_0_9; -.
DR   OrthoDB; 692853at2; -.
DR   Proteomes; UP000000596; Chromosome.
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_0000045223"
SQ   SEQUENCE   315 AA;  35642 MW;  F4D0FD71E4BE534B CRC64;
     MLKNKILATT LSVSLLAPLA NPLLENAKAA NDTEDIGKGN DVEIIKRTED KTSNKWGVTQ
     NIQFDFVKDK KYNKDALILK MQGFISSRTT YYNYKNTNHI KSMRWPFQYN IGLKTNDKYV
     SLINYLPKNK IESTNVSQTL GYNIGGNFQS APSLGGNGSF NYSKSISYTQ QNYVSEVEQQ
     NSKSVLWGVK ANSFATESGQ KSAFDSDLFV GYKPHSKDPR DYFVPDSELP PLVQSGFNPS
     FIATVSHEKG SSDTSEFEIT YGRNMDVTHA IKRSTHYGNS YLDGHRVHNA FKNRNYTVKY
     EVNWKTHEIK VKGQN