SPEB_STRPQ
ID SPEB_STRPQ Reviewed; 398 AA.
AC P0DD39; P00788; P26296; P68884; Q54960; Q54961; Q54962; Q54963; Q54964;
AC Q54965; Q54966; Q54967; Q54968; Q57024; Q57082; Q57202; Q57211; Q57212;
AC Q9S680;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Streptopain;
DE EC=3.4.22.10;
DE AltName: Full=Exotoxin type B;
DE AltName: Full=SPE B;
DE AltName: Full=Streptococcal cysteine proteinase;
DE AltName: Full=Streptococcus peptidase A;
DE Short=SPP;
DE Flags: Precursor;
GN Name=speB; OrderedLocusNames=SPs1739;
OS Streptococcus pyogenes serotype M3 (strain SSI-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=193567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSI-1;
RX PubMed=12799345; DOI=10.1101/gr.1096703;
RA Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA Hattori M., Hamada S.;
RT "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT scale genomic rearrangement in invasive strains and new insights into phage
RT evolution.";
RL Genome Res. 13:1042-1055(2003).
CC -!- FUNCTION: Important streptococcal virulence factor which cleaves human
CC fibronectin and degrades vitronectin. Also cleaves human IL1B precursor
CC to form biologically active IL1B. Can induce apoptosis in human
CC monocytes and epithelial cells in vitro, and reduces phagocytic
CC activity in monocytic cells. Thus, may play a role in bacterial
CC colonization, invasion, and inhibition of wound healing (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage with hydrophobic residues at P2, P1 and
CC P1'.; EC=3.4.22.10;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C10 family. {ECO:0000305}.
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DR EMBL; BA000034; BAC64834.1; -; Genomic_DNA.
DR RefSeq; WP_002991253.1; NC_004606.1.
DR AlphaFoldDB; P0DD39; -.
DR BMRB; P0DD39; -.
DR SMR; P0DD39; -.
DR MEROPS; C10.001; -.
DR KEGG; sps:SPs1739; -.
DR HOGENOM; CLU_716727_0_0_9; -.
DR OMA; WESQIDK; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.50; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000200; Peptidase_C10.
DR InterPro; IPR025896; Spi_Prtas-inh.
DR InterPro; IPR044934; Streptopain_sf.
DR Pfam; PF13734; Inhibitor_I69; 1.
DR Pfam; PF01640; Peptidase_C10; 1.
DR PRINTS; PR00797; STREPTOPAIN.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 3: Inferred from homology;
KW Hydrolase; Methylation; Protease; Secreted; Signal; Thiol protease; Toxin;
KW Virulence; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT PROPEP 28..145
FT /evidence="ECO:0000250"
FT /id="PRO_0000411458"
FT CHAIN 146..398
FT /note="Streptopain"
FT /id="PRO_0000411459"
FT ACT_SITE 192
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT MOD_RES 192
FT /note="Cysteine methyl disulfide; in zymogen form"
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 43174 MW; 16FF180D720AEE0F CRC64;
MNKKKLGIRL LSLLALGGFV LANPVFADQN FARNEKEAKD SAITFIQKSA AIKAGARSAE
DIKLDKVNLG GELSGSNMYV YNISTGGFVI VSGDKRSPEI LGYSTSGSFD ANGKENIASF
MESYVEQIKE NKKLDTTYAG TAEIKQPVVK SLLDSKGIHY NQGNPYNLLT PVIEKVKPGE
QSFVGQHAAT GCVATATAQI MKYHNYPNKG LKDYTYTLSS NNPYFNHPKN LFAAISTRQY
NWNNILPTYS GRESNVQKMA ISELMADVGI SVDMDYGPSS GSAGSSRVQR ALKENFGYNQ
SVHQINRSDF SKQDWEAQID KELSQNQPVY YQGVGKVGGH AFVIDGADGR NFYHVNWGWG
GVSDGFFRLD ALNPSALGTG GGAGGFNGYQ SAVVGIKP