ID   SPEB_STRPM              Reviewed;         398 AA.
AC   Q48R29;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=M28_Spy1721;
OS   Streptococcus pyogenes serotype M28 (strain MGAS6180).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=319701;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=MGAS587 / Serotype M28;
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=MGAS6180;
RX   PubMed=16088825; DOI=10.1086/430618;
RA   Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B.,
RA   Lefebvre R.B., Musser J.M.;
RT   "Genome sequence of a serotype M28 strain of group A Streptococcus:
RT   potential new insights into puerperal sepsis and bacterial disease
RT   specificity.";
RL   J. Infect. Dis. 192:760-770(2005).
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.
CC   -!- SIMILARITY: Belongs to the peptidase C10 family. {ECO:0000305}.
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DR   EMBL; L26134; AAA27000.1; -; Genomic_DNA.
DR   EMBL; CP000056; AAX72831.1; -; Genomic_DNA.
DR   RefSeq; WP_011285235.1; NC_007296.2.
DR   AlphaFoldDB; Q48R29; -.
DR   SMR; Q48R29; -.
DR   MEROPS; C10.001; -.
DR   EnsemblBacteria; AAX72831; AAX72831; M28_Spy1721.
DR   KEGG; spb:M28_Spy1721; -.
DR   HOGENOM; CLU_716727_0_0_9; -.
DR   OMA; WESQIDK; -.
DR   Proteomes; UP000009292; 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_0000042664"
FT   CHAIN           146..398
FT                   /note="Streptopain"
FT                   /id="PRO_0000042665"
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"
FT   CONFLICT        293
FT                   /note="K -> R (in Ref. 1; AAA27000)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   398 AA;  43190 MW;  16E107EC8C150FEF 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 SKQDWESQID KELSQNQPVY YQGVGKVGGH AFVIDGADGR NFYHVNWGWG
     GVSDGFFRLD ALNPSALGTG GGAGGFNGYQ SAVVGIKP