HLGB_STAA8
ID HLGB_STAA8 Reviewed; 325 AA.
AC Q2FVK1;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Gamma-hemolysin component B;
DE AltName: Full=H-gamma-1;
DE AltName: Full=H-gamma-I;
DE AltName: Full=Leukocidin f subunit;
DE Flags: Precursor;
GN Name=hlgB; OrderedLocusNames=SAOUHSC_02710;
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 mutant (at protein
CC level). {ECO:0000269|PubMed:20472795}.
CC -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
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DR EMBL; CP000253; ABD31718.1; -; Genomic_DNA.
DR RefSeq; WP_000783428.1; NZ_LS483365.1.
DR RefSeq; YP_501172.1; NC_007795.1.
DR AlphaFoldDB; Q2FVK1; -.
DR SMR; Q2FVK1; -.
DR STRING; 1280.SAXN108_2677; -.
DR EnsemblBacteria; ABD31718; ABD31718; SAOUHSC_02710.
DR GeneID; 3919729; -.
DR KEGG; sao:SAOUHSC_02710; -.
DR PATRIC; fig|93061.5.peg.2454; -.
DR eggNOG; ENOG50348U0; Bacteria.
DR HOGENOM; CLU_055394_0_1_9; -.
DR OMA; QNAKTHT; -.
DR PRO; PR:Q2FVK1; -.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..325
FT /note="Gamma-hemolysin component B"
FT /id="PRO_0000414601"
SQ SEQUENCE 325 AA; 36711 MW; 082999EB9339B6A0 CRC64;
MKMNKLVKSS VATSMALLLL SGTANAEGKI TPVSVKKVDD KVTLYKTTAT ADSDKFKISQ
ILTFNFIKDK SYDKDTLVLK ATGNINSGFV KPNPNDYDFS KLYWGAKYNV SISSQSNDSV
NVVDYAPKNQ NEEFQVQNTL GYTFGGDISI SNGLSGGLNG NTAFSETINY KQESYRTTLS
RNTNYKNVGW GVEAHKIMNN GWGPYGRDSF HPTYGNELFL AGRQSSAYAG QNFIAQHQMP
LLSRSNFNPE FLSVLSHRQD GAKKSKITVT YQREMDLYQI RWNGFYWAGA NYKNFKTRTF
KSTYEIDWEN HKVKLLDTKE TENNK