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Streptopain (EC 3.4.22.10) (Exotoxin type B) (SPE B) (Streptococcal cysteine proteinase) (Streptococcus peptidase A) (SPP)

 SPEB_STRP8              Reviewed;         398 AA.
P68885; P00788; P26296; Q54960; Q54961; Q54962; Q54963; Q54964;
Q54965; Q54966; Q54967; Q54968; Q57024; Q57082; Q57202; Q57211;
Q57212; Q9S680;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 1.
22-NOV-2017, entry version 65.
RecName: Full=Streptopain;
EC=3.4.22.10;
AltName: Full=Exotoxin type B;
AltName: Full=SPE B;
AltName: Full=Streptococcal cysteine proteinase;
AltName: Full=Streptococcus peptidase A;
Short=SPP;
Flags: Precursor;
Name=speB; OrderedLocusNames=spyM18_2099;
Streptococcus pyogenes serotype M18 (strain MGAS8232).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=186103;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
STRAIN=156 / Serotype M18, and 300 / Serotype M18;
PubMed=7516997; DOI=10.1006/mpat.1993.1083;
Kapur V., Topouzis S., Majesky M.W., Li L.L., Hamrick M.R.,
Hamill R.J., Patti J.M., Musser J.M.;
"A conserved Streptococcus pyogenes extracellular cysteine protease
cleaves human fibronectin and degrades vitronectin.";
Microb. Pathog. 15:327-346(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MGAS8232;
PubMed=11917108; DOI=10.1073/pnas.062526099;
Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F.,
Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q.,
Kapur V., Daly J.A., Veasy L.G., Musser J.M.;
"Genome sequence and comparative microarray analysis of serotype M18
group A Streptococcus strains associated with acute rheumatic fever
outbreaks.";
Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
-!- FUNCTION: Important streptococcal virulence factor which cleaves
human fibronectin and degrades vitronectin. Also cleaves human
IL1B precursor to form biologically active IL1B. Can induce
apoptosis in human monocytes and epithelial cells in vitro, and
reduces phagocytic activity in monocytic cells. Thus, may play a
role in bacterial colonization, invasion, and inhibition of wound
healing.
-!- CATALYTIC ACTIVITY: Preferential cleavage with hydrophobic
residues at P2, P1 and P1'.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the peptidase C10 family. {ECO:0000305}.
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EMBL; L26125; AAA26979.1; -; Genomic_DNA.
EMBL; AE009949; AAL98559.1; -; Genomic_DNA.
RefSeq; WP_002991253.1; NC_003485.1.
ProteinModelPortal; P68885; -.
SMR; P68885; -.
EnsemblBacteria; AAL98559; AAL98559; spyM18_2099.
KEGG; spm:spyM18_2099; -.
KO; K01364; -.
OMA; WESQIDK; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR000200; Peptidase_C10.
InterPro; IPR025896; Spi_Prtas-inh.
Pfam; PF13734; Inhibitor_I69; 1.
Pfam; PF01640; Peptidase_C10; 1.
PRINTS; PR00797; STREPTOPAIN.
ProDom; PD004169; Peptidase_C10; 1.
1: Evidence at protein level;
Hydrolase; Methylation; Protease; Secreted; Signal; Thiol protease;
Toxin; Virulence; Zymogen.
SIGNAL 1 27 {ECO:0000250}.
PROPEP 28 145 {ECO:0000250}.
/FTId=PRO_0000028509.
CHAIN 146 398 Streptopain.
/FTId=PRO_0000028510.
ACT_SITE 192 192 Nucleophile. {ECO:0000250}.
ACT_SITE 340 340 Proton acceptor. {ECO:0000250}.
MOD_RES 192 192 Cysteine methyl disulfide; in zymogen
form. {ECO:0000250}.
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


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