位置:首页 > 蛋白库 > SSL5_STAA8
SSL5_STAA8
ID   SSL5_STAA8              Reviewed;         234 AA.
AC   Q2G1S6;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Staphylococcal superantigen-like 5 {ECO:0000303|PubMed:17132726};
DE   Flags: Precursor;
GN   Name=ssl5 {ECO:0000303|PubMed:17132726}; OrderedLocusNames=SAOUHSC_00390;
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 HOST SELPLG.
RC   STRAIN=NCTC 8325 / PS 47;
RX   PubMed=17132726; DOI=10.1182/blood-2006-06-015461;
RA   Bestebroer J., Poppelier M.J., Ulfman L.H., Lenting P.J., Denis C.V.,
RA   van Kessel K.P., van Strijp J.A., de Haas C.J.;
RT   "Staphylococcal superantigen-like 5 binds PSGL-1 and inhibits P-selectin-
RT   mediated neutrophil rolling.";
RL   Blood 109:2936-2943(2007).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH HOST MMP9.
RC   STRAIN=ATCC 27733;
RX   PubMed=20479083; DOI=10.1128/iai.00178-10;
RA   Itoh S., Hamada E., Kamoshida G., Takeshita K., Oku T., Tsuji T.;
RT   "Staphylococcal superantigen-like protein 5 inhibits matrix
RT   metalloproteinase 9 from human neutrophils.";
RL   Infect. Immun. 78:3298-3305(2010).
RN   [4]
RP   FUNCTION, INTERACTION WITH HOST GP1BA AND GP6, AND MUTAGENESIS OF THR-205.
RC   STRAIN=NCTC 8325 / PS 47;
RX   PubMed=21552524; DOI=10.1371/journal.pone.0019190;
RA   Hu H., Armstrong P.C., Khalil E., Chen Y.C., Straub A., Li M.,
RA   Soosairajah J., Hagemeyer C.E., Bassler N., Huang D., Ahrens I.,
RA   Krippner G., Gardiner E., Peter K.;
RT   "GPVI and GPIbalpha mediate staphylococcal superantigen-like protein 5
RT   (SSL5) induced platelet activation and direct toward glycans as potential
RT   inhibitors.";
RL   PLoS ONE 6:E19190-E19190(2011).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH HOST MMP9.
RX   PubMed=29462623; DOI=10.1016/j.bbrc.2018.02.138;
RA   Kohno K., Itoh S., Hanai A., Takii T., Fujiwara T., Onozaki K., Tsuji T.,
RA   Hida S.;
RT   "Identification of matrix metalloproteinase 9-interacting sequences in
RT   staphylococcal superantigen-like protein 5.";
RL   Biochem. Biophys. Res. Commun. 497:713-718(2018).
RN   [6]
RP   INTERACTION WITH HOST MMP9.
RX   PubMed=29328525; DOI=10.1111/1348-0421.12573;
RA   Kurisaka C., Oku T., Itoh S., Tsuji T.;
RT   "Role of sialic acid-containing glycans of matrix metalloproteinase-9 (MMP-
RT   9) in the interaction between MMP-9 and staphylococcal superantigen-like
RT   protein 5.";
RL   Microbiol. Immunol. 62:168-175(2018).
CC   -!- FUNCTION: Secreted protein that plays a role in the inhibition of host
CC       innate immune system. Modulates the interaction between host SELPLG and
CC       P-selectin thereby preventing initial rolling of neutrophils toward the
CC       site of infection (PubMed:17132726). Interferes with leukocyte
CC       trafficking by inhibiting host metalloproteinase-9/MMP9 activity
CC       (PubMed:20479083, PubMed:29462623, PubMed:29328525). Associates also
CC       with two different platelet surface receptors GP1A and GP6 leading to
CC       platelet activation and aggregation (PubMed:21552524).
CC       {ECO:0000269|PubMed:17132726, ECO:0000269|PubMed:20479083,
CC       ECO:0000269|PubMed:21552524, ECO:0000269|PubMed:29328525,
CC       ECO:0000269|PubMed:29462623}.
CC   -!- SUBUNIT: Interacts with host SELPLG; this interaction prevents SELPLG-
CC       mediated neutrophil rolling (PubMed:17132726). Interacts with host MMP9
CC       (via sialic acid-containing O-glycans); this interaction inhibits MMP9
CC       activity. Interacts with host GP1BA and GP6; these interactions play an
CC       important role in platelet binding and activation (PubMed:21552524).
CC       {ECO:0000269|PubMed:17132726, ECO:0000269|PubMed:21552524}.
CC   -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000253; ABD29553.1; -; Genomic_DNA.
DR   RefSeq; WP_000784244.1; NZ_LS483365.1.
DR   RefSeq; YP_498976.1; NC_007795.1.
DR   AlphaFoldDB; Q2G1S6; -.
DR   SMR; Q2G1S6; -.
DR   STRING; 1280.SAXN108_0481; -.
DR   EnsemblBacteria; ABD29553; ABD29553; SAOUHSC_00390.
DR   GeneID; 3919125; -.
DR   KEGG; sao:SAOUHSC_00390; -.
DR   PATRIC; fig|93061.5.peg.358; -.
DR   eggNOG; ENOG503054K; Bacteria.
DR   HOGENOM; CLU_054950_1_0_9; -.
DR   OMA; YIYKEEV; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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   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   Reference proteome; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..234
FT                   /note="Staphylococcal superantigen-like 5"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004207838"
FT   MUTAGEN         205
FT                   /note="T->P: Complete loss of interaction with GP1BA."
FT                   /evidence="ECO:0000269|PubMed:21552524"
SQ   SEQUENCE   234 AA;  27170 MW;  B8D2BA9C7FEC2CE9 CRC64;
     MKMTAIAKAS LALGILATGT ITSLHQTVNA SEHKAKYENV TKDIFDLRDY YSGASKELKN
     VTGYRYSKGG KHYLIFDKNR KFTRVQIFGK DIERFKARKN PGLDIFVVKE AENRNGTVFS
     YGGVTKKNQD AYYDYINAPR FQIKRDEGDG IATYGRVHYI YKEEISLKEL DFKLRQYLIQ
     NFDLYKKFPK DSKIKVIMKD GGYYTFELNK KLQTNRMSDV IDGRNIEKIE ANIR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024