ID   SSL7_STAAE              Reviewed;         231 AA.
AC   A0A0H3K6Z8;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Staphylococcal superantigen-like 7 {ECO:0000303|PubMed:23797068};
DE   Flags: Precursor;
GN   Name=ssl7 {ECO:0000303|PubMed:23797068}; OrderedLocusNames=NWMN_0394;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH COMPLEMENT C5 AND IGA.
RC   STRAIN=Newman;
RX   PubMed=23797068; DOI=10.1038/icb.2013.28;
RA   Lorenz N., Clow F., Radcliff F.J., Fraser J.D.;
RT   "Full functional activity of SSL7 requires binding of both complement C5
RT   and IgA.";
RL   Immunol. Cell Biol. 91:469-476(2013).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (4.20 ANGSTROMS) OF 129-231, FUNCTION, AND
RP   INTERACTION WITH COMPLEMENT C5 AND IGA.
RX   PubMed=20133685; DOI=10.1073/pnas.0910565107;
RA   Laursen N.S., Gordon N., Hermans S., Lorenz N., Jackson N., Wines B.,
RA   Spillner E., Christensen J.B., Jensen M., Fredslund F., Bjerre M.,
RA   Sottrup-Jensen L., Fraser J.D., Andersen G.R.;
RT   "Structural basis for inhibition of complement C5 by the SSL7 protein from
RT   Staphylococcus aureus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:3681-3686(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:23797068). 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 (By similarity). {ECO:0000250|UniProtKB:Q2G2Y0,
CC       ECO:0000269|PubMed:23797068}.
CC   -!- SUBUNIT: Interacts with host IgA and complement C5.
CC       {ECO:0000269|PubMed:20133685, ECO:0000269|PubMed:23797068}.
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; AP009351; BAF66666.1; -; Genomic_DNA.
DR   RefSeq; WP_000769836.1; NZ_CP023390.1.
DR   PDB; 3KM9; X-ray; 4.20 A; X/Y=129-231.
DR   PDBsum; 3KM9; -.
DR   AlphaFoldDB; A0A0H3K6Z8; -.
DR   SMR; A0A0H3K6Z8; -.
DR   EnsemblBacteria; BAF66666; BAF66666; NWMN_0394.
DR   KEGG; sae:NWMN_0394; -.
DR   HOGENOM; CLU_054950_1_0_9; -.
DR   OMA; GQNHQLF; -.
DR   Proteomes; UP000006386; 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   3D-structure; Secreted; Signal; Virulence.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..231
FT                   /note="Staphylococcal superantigen-like 7"
FT                   /id="PRO_0000447560"
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