ID   SPEB_STRP6              Reviewed;         398 AA.
AC   Q5X9P3; P00788; P26296; Q54960; Q54961; Q54962; Q54963; Q54964; Q54965;
AC   Q54966; Q54967; Q54968; Q57024; Q57082; Q57202; Q57211; Q57212; Q9S680;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=M6_Spy1735;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=303 / Serotype M6;
RX   PubMed=7516997; DOI=10.1006/mpat.1993.1083;
RA   Kapur V., Topouzis S., Majesky M.W., Li L.L., Hamrick M.R., Hamill R.J.,
RA   Patti J.M., Musser J.M.;
RT   "A conserved Streptococcus pyogenes extracellular cysteine protease cleaves
RT   human fibronectin and degrades vitronectin.";
RL   Microb. Pathog. 15:327-346(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
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.
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.
CC   -!- SIMILARITY: Belongs to the peptidase C10 family. {ECO:0000305}.
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DR   EMBL; CP000003; AAT87870.1; -; Genomic_DNA.
DR   RefSeq; WP_002991253.1; NC_006086.1.
DR   AlphaFoldDB; Q5X9P3; -.
DR   SMR; Q5X9P3; -.
DR   MEROPS; C10.001; -.
DR   EnsemblBacteria; AAT87870; AAT87870; M6_Spy1735.
DR   KEGG; spa:M6_Spy1735; -.
DR   HOGENOM; CLU_716727_0_0_9; -.
DR   OMA; WESQIDK; -.
DR   Proteomes; UP000001167; Chromosome.
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   1: Evidence at protein level;
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_0000028507"
FT   CHAIN           146..398
FT                   /note="Streptopain"
FT                   /id="PRO_0000028508"
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