ID   SSL7_STAA8              Reviewed;         231 AA.
AC   Q2G2Y0;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Staphylococcal superantigen-like 7 {ECO:0000303|PubMed:15728504};
DE   Flags: Precursor;
GN   Name=ssl7 {ECO:0000303|PubMed:15728504}; OrderedLocusNames=SAOUHSC_00392;
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   FUNCTION, AND INTERACTION WITH HOST COMPLEMENT C5.
RC   STRAIN=GL1;
RX   PubMed=15728504; DOI=10.4049/jimmunol.174.5.2926;
RA   Langley R., Wines B., Willoughby N., Basu I., Proft T., Fraser J.D.;
RT   "The staphylococcal superantigen-like protein 7 binds IgA and complement C5
RT   and inhibits IgA-Fc alpha RI binding and serum killing of bacteria.";
RL   J. Immunol. 174:2926-2933(2005).
RN   [3]
RP   FUNCTION, INTERACTION WITH HOST COMPLEMENT C5, AND MUTAGENESIS OF ASN-68;
RP   LEU-109; PRO-112 AND ASP-147.
RC   STRAIN=NCTC 8325 / PS 47;
RX   PubMed=20545943; DOI=10.1111/j.1462-5822.2010.01486.x;
RA   Bestebroer J., Aerts P.C., Rooijakkers S.H., Pandey M.K., Koehl J.,
RA   van Strijp J.A., de Haas C.J.;
RT   "Functional basis for complement evasion by staphylococcal superantigen-
RT   like 7.";
RL   Cell. Microbiol. 12:1506-1516(2010).
CC   -!- FUNCTION: Plays a role in the inhibition of host complement-mediated
CC       lysis and serum bactericidal activity by interacting with complement
CC       component C5 (PubMed:15728504). Affects all three pathways of
CC       complement activation and inhibits the cleavage of C5 by preventing its
CC       binding to C5 convertases. In turn, prevents C5a-mediated neutrophil
CC       migration (PubMed:20545943). {ECO:0000269|PubMed:15728504,
CC       ECO:0000269|PubMed:20545943}.
CC   -!- SUBUNIT: Interacts with host IgA and complement C5; these interactions
CC       inhibits complement activation. {ECO:0000269|PubMed:15728504,
CC       ECO:0000269|PubMed:20545943}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q2G1S8}.
CC   -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC       {ECO:0000305}.
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DR   EMBL; CP000253; ABD29555.1; -; Genomic_DNA.
DR   RefSeq; WP_000769836.1; NZ_LS483365.1.
DR   RefSeq; YP_498979.1; NC_007795.1.
DR   AlphaFoldDB; Q2G2Y0; -.
DR   SMR; Q2G2Y0; -.
DR   STRING; 1280.SAXN108_0483; -.
DR   EnsemblBacteria; ABD29555; ABD29555; SAOUHSC_00392.
DR   GeneID; 3919127; -.
DR   KEGG; sao:SAOUHSC_00392; -.
DR   PATRIC; fig|93061.5.peg.360; -.
DR   eggNOG; ENOG503054K; Bacteria.
DR   HOGENOM; CLU_054950_1_0_9; -.
DR   OMA; GQNHQLF; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008992; Enterotoxin.
DR   InterPro; IPR015282; SSL_OB.
DR   InterPro; IPR006126; Staph/Strept_toxin_CS.
DR   InterPro; IPR008375; Staph_exotoxin.
DR   InterPro; IPR016091; SuperAg_toxin_C.
DR   InterPro; IPR013307; Superantigen_bac.
DR   InterPro; IPR006123; Toxin_b-grasp_Staph/Strep.
DR   Pfam; PF09199; SSL_OB; 1.
DR   Pfam; PF02876; Stap_Strp_tox_C; 1.
DR   PRINTS; PR01898; SAGSUPRFAMLY.
DR   PRINTS; PR01800; STAPHEXOTOXN.
DR   PRINTS; PR01501; TOXICSSTOXIN.
DR   SUPFAM; SSF50203; SSF50203; 1.
DR   SUPFAM; SSF54334; SSF54334; 1.
DR   PROSITE; PS00278; STAPH_STREP_TOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..231
FT                   /note="Staphylococcal superantigen-like 7"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5002613391"
FT   MUTAGEN         68
FT                   /note="N->Y: Loss of host IgA binding; when associated with
FT                   A-109 and A-112."
FT                   /evidence="ECO:0000269|PubMed:20545943"
FT   MUTAGEN         109
FT                   /note="L->A: Loss of host IgA binding; when associated with
FT                   Y-68 and A-112."
FT                   /evidence="ECO:0000269|PubMed:20545943"
FT   MUTAGEN         112
FT                   /note="P->A: Loss of host IgA binding; when associated with
FT                   Y-68 and A-109."
FT                   /evidence="ECO:0000269|PubMed:20545943"
FT   MUTAGEN         147
FT                   /note="D->K: Loss of host complement C5 binding."
FT                   /evidence="ECO:0000269|PubMed:20545943"
SQ   SEQUENCE   231 AA;  26168 MW;  8B9F437C0BB33E66 CRC64;
     MKLKTLAKAT LALGLLTTGV ITSEGQAVQA KEKQERVQHL YDIKDLHRYY SSESFEFSNI
     SGKVENYNGS NVVRFNQENQ NHQLFLLGKD KEKYKEGIEG KDVFVVKELI DPNGRLSTVG
     GVTKKNNKSS ETNTHLFVNK VYGGNLDASI DSFSINKEEV SLKELDFKIR QHLVKNYGLY
     KGTTKYGKIT INLKDGEKQE IDLGDKLQFE RMGDVLNSKD INKIEVTLKQ I