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   16-JUN-2009, entry version 23.
DE   RecName: Full=Streptopain;
DE            EC=3.4.22.10;
DE   AltName: Full=Streptococcal cysteine proteinase;
DE   AltName: Full=Streptococcus peptidase A;
DE            Short=SPP;
DE   AltName: Full=Exotoxin type B;
DE   AltName: Full=SPE B;
DE   Flags: Precursor;
GN   Name=speB; OrderedLocusNames=M28_Spy1721;
OS   Streptococcus pyogenes serotype M28.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=319700;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=MGAS587 / Serotype M28;
RX   MEDLINE=94285789; PubMed=7516997; DOI=10.1006/mpat.1993.1083;
RA   Kapur V., Topouzis S., Majesky M.W., Li L.L., Hamrick M.R.,
RA   Hamill R.J., Patti J.M., Musser J.M.;
RT   "A conserved Streptococcus pyogenes extracellular cysteine protease
RT   cleaves human fibronectin and degrades vitronectin.";
RL   Microb. Pathog. 15:327-346(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS6180 / Serotype M28;
RX   PubMed=16088825; DOI=10.1086/430618;
RA   Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D.,
RA   Beres S.B., 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
CC       human fibronectin and degrades vitronectin. Also cleaves human
CC       IL1B precursor to form biologically active IL1B. Can induce
CC       apoptosis in human monocytes and epithelial cells in vitro, and
CC       reduces phagocytic activity in monocytic cells. Thus, may play a
CC       role in bacterial colonization, invasion, and inhibition of wound
CC       healing (By similarity).
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage with hydrophobic
CC       residues at P2, P1 and P1'.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase C10 family.
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DR   EMBL; L26134; AAA27000.1; -; Genomic_DNA.
DR   EMBL; CP000056; AAX72831.1; -; Genomic_DNA.
DR   RefSeq; YP_281186.1; -.
DR   SMR; Q48R29; 31-398.
DR   GeneID; 3574450; -.
DR   GenomeReviews; CP000056_GR; M28_Spy1721.
DR   KEGG; spb:M28_Spy1721; -.
DR   HOGENOM; Q48R29; -.
DR   OMA; Q48R29; WESQIDK.
DR   BioCyc; SPYO319701:M28_SPY1721-MON; -.
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:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000200; Peptidase_C10.
DR   Pfam; PF01640; Peptidase_C10; 1.
DR   PRINTS; PR00797; STREPTOPAIN.
DR   ProDom; PD004169; Peptidase_C10; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Hydrolase; Methylation; Protease; Secreted; Signal;
KW   Thiol protease; Toxin; Virulence; Zymogen.
FT   SIGNAL        1     27       By similarity.
FT   PROPEP       28    145       By similarity.
FT                                /FTId=PRO_0000042664.
FT   CHAIN       146    398       Streptopain.
FT                                /FTId=PRO_0000042665.
FT   ACT_SITE    192    192       By similarity.
FT   ACT_SITE    340    340       By similarity.
FT   MOD_RES     192    192       Cysteine methyl disulfide; in zymogen
FT                                form (By similarity).
FT   CONFLICT    293    293       K -> R (in Ref. 1; AAA27000).
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
//