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SSL10_STAA8
ID   SSL10_STAA8             Reviewed;         227 AA.
AC   Q2G2X7;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Staphylococcal superantigen-like 10 {ECO:0000303|PubMed:19308288};
DE   Flags: Precursor;
GN   Name=ssl10 {ECO:0000303|PubMed:19308288}; OrderedLocusNames=SAOUHSC_00395;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH HUMAN CXCR4.
RC   STRAIN=NCTC 8325 / PS 47;
RX   PubMed=19308288; DOI=10.1593/neo.81508;
RA   Walenkamp A.M., Boer I.G., Bestebroer J., Rozeveld D., Timmer-Bosscha H.,
RA   Hemrika W., van Strijp J.A., de Haas C.J.;
RT   "Staphylococcal superantigen-like 10 inhibits CXCL12-induced human tumor
RT   cell migration.";
RL   Neoplasia 11:333-344(2009).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC 277933;
RX   PubMed=19913916; DOI=10.1016/j.molimm.2009.09.027;
RA   Itoh S., Hamada E., Kamoshida G., Yokoyama R., Takii T., Onozaki K.,
RA   Tsuji T.;
RT   "Staphylococcal superantigen-like protein 10 (SSL10) binds to human
RT   immunoglobulin G (IgG) and inhibits complement activation via the classical
RT   pathway.";
RL   Mol. Immunol. 47:932-938(2010).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH HOST PROTHROMBIN/F2.
RC   STRAIN=ATCC 277933;
RX   PubMed=23754290; DOI=10.1074/jbc.m113.451419;
RA   Itoh S., Yokoyama R., Kamoshida G., Fujiwara T., Okada H., Takii T.,
RA   Tsuji T., Fujii S., Hashizume H., Onozaki K.;
RT   "Staphylococcal superantigen-like protein 10 (SSL10) inhibits blood
RT   coagulation by binding to prothrombin and factor Xa via their gamma-
RT   carboxyglutamic acid (Gla) domain.";
RL   J. Biol. Chem. 288:21569-21580(2013).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH HOST PROTHROMBIN/F2.
RC   STRAIN=ATCC 277933;
RX   PubMed=28193526; DOI=10.1016/j.bbrc.2017.02.053;
RA   Itoh S., Takii T., Onozaki K., Tsuji T., Hida S.;
RT   "Identification of the blood coagulation factor interacting sequences in
RT   staphylococcal superantigen-like protein 10.";
RL   Biochem. Biophys. Res. Commun. 485:201-208(2017).
CC   -!- FUNCTION: Plays a role in the inhibition of host complement activation
CC       via the classical pathway by interacting with the Fc region of human
CC       IgG and thereby interfering with the IgG/C1q interaction
CC       (PubMed:19913916). Inhibits also the penultimate step of plasma
CC       clotting by interacting with prothrombin/F2 and coagulation factor
CC       X/F12. Does not affect the protease activity of thrombin but interferes
CC       with the conversion of prothrombin to thrombin (PubMed:23754290,
CC       PubMed:28193526). Interacts with human receptor CXCR4 and specifically
CC       inhibits CXCL12-induced calcium mobilization and cell migration
CC       (PubMed:19308288). {ECO:0000269|PubMed:19308288,
CC       ECO:0000269|PubMed:19913916, ECO:0000269|PubMed:23754290,
CC       ECO:0000269|PubMed:28193526}.
CC   -!- SUBUNIT: Interacts with prothrombin/F2 and coagulation factor X/F12
CC       (PubMed:23754290, PubMed:28193526). Interacts with human CXCR4
CC       (PubMed:19308288). {ECO:0000269|PubMed:19308288,
CC       ECO:0000269|PubMed:23754290, ECO:0000269|PubMed:28193526}.
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; CP000253; ABD29558.1; -; Genomic_DNA.
DR   RefSeq; WP_000673051.1; NZ_LS483365.1.
DR   RefSeq; YP_498982.1; NC_007795.1.
DR   PDB; 6LWT; X-ray; 1.90 A; A/B=31-227.
DR   PDB; 6UCD; X-ray; 2.85 A; A/B=30-227.
DR   PDBsum; 6LWT; -.
DR   PDBsum; 6UCD; -.
DR   AlphaFoldDB; Q2G2X7; -.
DR   SMR; Q2G2X7; -.
DR   STRING; 1280.SAXN108_0486; -.
DR   EnsemblBacteria; ABD29558; ABD29558; SAOUHSC_00395.
DR   GeneID; 3919130; -.
DR   KEGG; sao:SAOUHSC_00395; -.
DR   PATRIC; fig|93061.5.peg.363; -.
DR   HOGENOM; CLU_054950_1_0_9; -.
DR   OMA; NINALKH; -.
DR   Proteomes; UP000008816; 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; Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..227
FT                   /note="Staphylococcal superantigen-like 10"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004207952"
FT   HELIX           41..49
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          53..64
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   HELIX           84..89
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          92..103
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          112..117
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          119..122
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          133..137
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:6UCD"
FT   STRAND          147..150
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          155..159
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   HELIX           160..175
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   TURN            177..179
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          186..191
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          196..200
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          213..215
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   HELIX           216..218
FT                   /evidence="ECO:0007829|PDB:6LWT"
FT   STRAND          219..225
FT                   /evidence="ECO:0007829|PDB:6LWT"
SQ   SEQUENCE   227 AA;  26111 MW;  732955609D2333DD CRC64;
     MKFTALAKAT LALGILTTGT LTTEVHSGHA KQNQKSVNKH DKEALYRYYT GKTMEMKNIS
     ALKHGKNNLR FKFRGIKIQV LLPGNDKSKF QQRSYEGLDV FFVQEKRDKH DIFYTVGGVI
     QNNKTSGVVS APILNISKEK GEDAFVKGYP YYIKKEKITL KELDYKLRKH LIEKYGLYKT
     ISKDGRVKIS LKDGSFYNLD LRSKLKFKYM GEVIESKQIK DIEVNLK
 
 
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