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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
 
 
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