SSL3_STAAE
ID SSL3_STAAE Reviewed; 352 AA.
AC A0A0H3KEE1;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Staphylococcal superantigen-like 3 {ECO:0000250|UniProtKB:Q2G0X7};
DE Flags: Precursor;
GN Name=ssl3 {ECO:0000250|UniProtKB:Q2G0X7}; OrderedLocusNames=NWMN_0390;
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).
CC -!- FUNCTION: Secreted protein that plays an essential role in immune
CC innate response inhibition by interacting with and inhibiting host
CC TLR2. In turn, bacteria recognition by immune cells is impaired and
CC cytokine production is inhibited. Mechanistically, by interacting with
CC TLR2, blocks ligand binding and thus inhibits activation. Second, by
CC interacting with an already formed TLR2-lipopeptide complex, prevents
CC TLR heterodimerization and downstream signaling. The interaction with
CC host TLR2 does not involve sialyl Lewis X interactions.
CC {ECO:0000250|UniProtKB:Q2G0X7}.
CC -!- SUBUNIT: Interacts with host TLR2 (via its extracellular domain).
CC {ECO:0000250|UniProtKB:Q2G0X7}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q2G0X7}.
CC -!- DOMAIN: The C-terminal domain contains a V-shape binding site for
CC sialyl Lewis X. {ECO:0000250|UniProtKB:Q2G0X7}.
CC -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC {ECO:0000305}.
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DR EMBL; AP009351; BAF66662.1; -; Genomic_DNA.
DR RefSeq; WP_000784024.1; NZ_CP023390.1.
DR AlphaFoldDB; A0A0H3KEE1; -.
DR SMR; A0A0H3KEE1; -.
DR EnsemblBacteria; BAF66662; BAF66662; NWMN_0390.
DR KEGG; sae:NWMN_0390; -.
DR HOGENOM; CLU_054950_1_0_9; -.
DR OMA; FMNVIPD; -.
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 Pfam; PF09199; SSL_OB; 1.
DR PRINTS; PR01898; SAGSUPRFAMLY.
DR PRINTS; PR01800; STAPHEXOTOXN.
DR SUPFAM; SSF50203; SSF50203; 1.
DR SUPFAM; SSF54334; SSF54334; 1.
DR PROSITE; PS00278; STAPH_STREP_TOXIN_2; 1.
PE 3: Inferred from homology;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..352
FT /note="Staphylococcal superantigen-like 3"
FT /evidence="ECO:0000255"
FT /id="PRO_5002613612"
FT REGION 61..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..326
FT /note="Sialyl Lewis X-binding"
FT /evidence="ECO:0000250|UniProtKB:Q2G0X7"
FT COMPBIAS 71..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 352 AA; 39739 MW; 87D15E34C8878A4D CRC64;
MKMRTIAKTS LALGLLTTGA ITVTTQSVKA EKIQSTKVDK VPTLKAERLA MINITAGANS
ATTQAANTRQ ERTPKLEKAP NTNEEKTSAS KIEKISQPKQ EEQKTLNISA TPAPKQEQSQ
TTTESTTPKT KVTTPPSTNT PQPMQSTKSD TPQSPTIKQA QTDMTPKYED LRAYYTKPSF
EFEKQFGFML KPWTTVRFMN VIPNRFIYKI ALVGKDEKKY KDGPYDNIDV FIVLEDNKYQ
LKKYSVGGIT KTNSKKVNHK VELSITKKDN QGMISRDVSE YMITKEEISL KELDFKLRKQ
LIEKHNLYGN MGSGTIVIKM KNGGKYTFEL HKKLQEHRMA GTNIDNIEVN IK