SSL11_STAAE
ID SSL11_STAAE Reviewed; 225 AA.
AC A0A0H3KEE7;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Superantigen-like protein 11 {ECO:0000250|UniProtKB:A8E1U5};
DE Flags: Precursor;
GN Name=ssl11 {ECO:0000250|UniProtKB:A8E1U5}; OrderedLocusNames=NWMN_0400;
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 a role in the inhibition of host
CC immune system. Targets myeloid cells such as monocytes or granulocytes
CC through binding with sialyllactosamine-containing glycoproteins.
CC Prevents initial rolling of neutrophils toward the site of infection by
CC interacting with host SELPLG. Disrupts neutrophil motility by induction
CC of cell adhesion via interacting with glycans but independently of
CC SELPLG. {ECO:0000250|UniProtKB:A8E1U5}.
CC -!- SUBUNIT: Homodimer (via its C-terminal domain). Interacts with host
CC FCAR and SELPLG (via sialyl Lewis X). {ECO:0000250|UniProtKB:A8E1U5}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q2G1S8}.
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; BAF66672.1; -; Genomic_DNA.
DR RefSeq; WP_000769163.1; NZ_CP023390.1.
DR AlphaFoldDB; A0A0H3KEE7; -.
DR SMR; A0A0H3KEE7; -.
DR EnsemblBacteria; BAF66672; BAF66672; NWMN_0400.
DR KEGG; sae:NWMN_0400; -.
DR HOGENOM; CLU_054950_1_0_9; -.
DR OMA; DKANEYN; -.
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 3: Inferred from homology;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..225
FT /note="Superantigen-like protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_5002613384"
FT REGION 94..196
FT /note="Sialyl Lewis X-binding"
FT /evidence="ECO:0000250|UniProtKB:Q2G0X7"
SQ SEQUENCE 225 AA; 25366 MW; 5ACE5CB6060D4150 CRC64;
MKLKNIAKAS LALGILTTGM ITTTAQPVKA STLEVRSQAT QDLSEYYNRP FFEYTNQSGY
KEEGKVTFTP NYQLIDVTLT GNEKQNFGED ISNVDIFVVR ENSDRSGNTA SIGGITKTNG
SNYIDKVKDV NLIITKNIDS VTSTSTSSTY TINKEEISLK ELDFKLRKHL IDKHNLYKTE
PKDSKIRITM KDGGFYTFEL NKKLQTHRMG DVIDGRNIEK IEVNL