SLL11_STAAU
ID SLL11_STAAU Reviewed; 196 AA.
AC A8E1U5;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Superantigen-like protein 11 {ECO:0000303|PubMed:18045383};
DE Flags: Fragment;
GN Name=sl11 {ECO:0000303|PubMed:18045383};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF
RP 1-196, SUBUNIT, INTERACTION WITH HOST SELPLG AND FCAR, AND MUTAGENESIS OF
RP THR-168.
RC STRAIN=US6610;
RX PubMed=18045383; DOI=10.1111/j.1365-2958.2007.05989.x;
RA Chung M.C., Wines B.D., Baker H., Langley R.J., Baker E.N., Fraser J.D.;
RT "The crystal structure of staphylococcal superantigen-like protein 11 in
RT complex with sialyl Lewis X reveals the mechanism for cell binding and
RT immune inhibition.";
RL Mol. Microbiol. 66:1342-1355(2007).
RN [2]
RP FUNCTION.
RC STRAIN=USA300_FPR3757;
RX PubMed=30862940; DOI=10.1038/s41598-019-40817-x;
RA Chen C., Yang C., Barbieri J.T.;
RT "Staphylococcal Superantigen-like protein 11 mediates neutrophil adhesion
RT and motility arrest, a unique bacterial toxin action.";
RL Sci. Rep. 9:4211-4211(2019).
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 (PubMed:18045383). Prevents initial rolling of neutrophils toward the
CC site of infection by interacting with host SELPLG (PubMed:18045383).
CC Disrupts neutrophil motility by induction of cell adhesion via
CC interacting with glycans but independently of SELPLG (PubMed:30862940).
CC {ECO:0000269|PubMed:18045383, ECO:0000269|PubMed:30862940}.
CC -!- SUBUNIT: Homodimer (via its C-terminal domain) (PubMed:18045383).
CC Interacts with host FCAR and SELPLG (via sialyl Lewis X)
CC (PubMed:18045383). {ECO:0000269|PubMed:18045383}.
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; AM887868; CAP09054.1; -; Genomic_DNA.
DR PDB; 2RDG; X-ray; 1.60 A; A=1-196.
DR PDB; 2RDH; X-ray; 1.70 A; A/B/C/D=1-196.
DR PDBsum; 2RDG; -.
DR PDBsum; 2RDH; -.
DR AlphaFoldDB; A8E1U5; -.
DR SMR; A8E1U5; -.
DR UniLectin; A8E1U5; -.
DR EvolutionaryTrace; A8E1U5; -.
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 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; Virulence.
FT CHAIN <1..196
FT /note="Superantigen-like protein 11"
FT /id="PRO_0000447510"
FT REGION 65..167
FT /note="Sialyl Lewis X-binding"
FT /evidence="ECO:0000250|UniProtKB:Q2G0X7"
FT MUTAGEN 168
FT /note="T->P: Complete loss of carbohydrate binding."
FT /evidence="ECO:0000269|PubMed:18045383"
FT NON_TER 1
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 21..32
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2RDG"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 59..70
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2RDG"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 98..108
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:2RDG"
FT HELIX 130..144
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2RDG"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2RDG"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2RDG"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:2RDG"
SQ SEQUENCE 196 AA; 22651 MW; 8B43EF30D11FF2DD CRC64;
STLEVRSQAT QDLSEYYNRP YFDLRNLSGY REGNTVTFIN HYQQTDVKLE GKDKDKIKDG
NNENLDVFVV REGSGRQADN NSIGGITKTN RTQHIDTVQN VNLLVSKSTG QHTTSVTSTN
YSIYKEEISL KELDFKLRKH LIDKHDLYKT EPKDSKIRVT MKNGDFYTFE LNKKLQTHRM
GDVIDGRNIE KIEVNL
