ID   HLGC_STAA8              Reviewed;         315 AA.
AC   Q2FVK2;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Gamma-hemolysin component C;
DE   AltName: Full=Leukocidin s subunit;
DE   Flags: Precursor;
GN   Name=hlgC; OrderedLocusNames=SAOUHSC_02709;
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   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: 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. HlgB (class F) associates with either hlgA
CC       thus forming an AB toxin or with hlgC thus forming a CB toxin (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20472795}.
CC   -!- INDUCTION: Less protein is secreted in a secG or double secG/secY2
CC       mutant (at protein level). {ECO:0000269|PubMed:20472795}.
CC   -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
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DR   EMBL; CP000253; ABD31717.1; -; Genomic_DNA.
DR   RefSeq; WP_000916713.1; NZ_LS483365.1.
DR   RefSeq; YP_501171.1; NC_007795.1.
DR   AlphaFoldDB; Q2FVK2; -.
DR   SMR; Q2FVK2; -.
DR   STRING; 1280.SAXN108_2676; -.
DR   EnsemblBacteria; ABD31717; ABD31717; SAOUHSC_02709.
DR   GeneID; 3919728; -.
DR   KEGG; sao:SAOUHSC_02709; -.
DR   PATRIC; fig|93061.5.peg.2453; -.
DR   eggNOG; ENOG5030531; Bacteria.
DR   HOGENOM; CLU_075311_0_0_9; -.
DR   PRO; PR:Q2FVK2; -.
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; 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   1: Evidence at protein level;
KW   Cytolysis; Hemolysis; Reference proteome; Secreted; Signal; Toxin;
KW   Virulence.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..315
FT                   /note="Gamma-hemolysin component C"
FT                   /id="PRO_0000414602"
SQ   SEQUENCE   315 AA;  35614 MW;  77359819736620BC CRC64;
     MLKNKILTTT LSVSLLAPLA NPLLENAKAA NDTEDIGKGS 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