SPEB_STRP1
ID SPEB_STRP1 Reviewed; 398 AA.
AC P0C0J1; P00788; P26296; P68883; Q48WC2; Q54960; Q54961; Q54962; Q54963;
AC Q54964; Q54965; Q54966; Q54967; Q54968; Q57024; Q57082; Q57202; Q57211;
AC Q57212; Q9S680;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=SPy_2039, M5005_Spy1735;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=789 / Serotype M1;
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 [GENOMIC DNA].
RC STRAIN=A-20 / Serotype M1,T1;
RA Wu J.-J.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [5]
RP FUNCTION.
RC STRAIN=A-20 / Serotype M1,T1;
RX PubMed=10456871; DOI=10.1128/iai.67.9.4334-4339.1999;
RA Tsai P.-J., Lin Y.-S., Kuo C.-F., Lei H.-Y., Wu J.-J.;
RT "Group A Streptococcus induces apoptosis in human epithelial cells.";
RL Infect. Immun. 67:4334-4339(1999).
RN [6]
RP STRUCTURE BY NMR OF 146-398, MUTAGENESIS OF VAL-334; TRP-357; TRP-359 AND
RP GLY-384, AND CATALYTIC ACTIVITY.
RX PubMed=19237546; DOI=10.1074/jbc.m807624200;
RA Wang C.C., Houng H.C., Chen C.L., Wang P.J., Kuo C.F., Lin Y.S., Wu J.J.,
RA Lin M.T., Liu C.C., Huang W., Chuang W.J.;
RT "Solution structure and backbone dynamics of streptopain: insight into
RT diverse substrate specificity.";
RL J. Biol. Chem. 284:10957-10967(2009).
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 {ECO:0000269|PubMed:10456871}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage with hydrophobic residues at P2, P1 and
CC P1'.; EC=3.4.22.10; Evidence={ECO:0000269|PubMed:19237546};
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; L26158; AAA26987.1; -; Genomic_DNA.
DR EMBL; AF104940; AAD17930.1; -; Genomic_DNA.
DR EMBL; AE004092; AAK34706.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ52353.1; -; Genomic_DNA.
DR RefSeq; NP_269985.1; NC_002737.2.
DR PDB; 2JTC; NMR; -; A=146-398.
DR PDBsum; 2JTC; -.
DR AlphaFoldDB; P0C0J1; -.
DR BMRB; P0C0J1; -.
DR SMR; P0C0J1; -.
DR STRING; 1314.HKU360_01851; -.
DR MEROPS; C10.001; -.
DR PaxDb; P0C0J1; -.
DR EnsemblBacteria; AAK34706; AAK34706; SPy_2039.
DR KEGG; spy:SPy_2039; -.
DR KEGG; spz:M5005_Spy1735; -.
DR PATRIC; fig|160490.10.peg.1768; -.
DR HOGENOM; CLU_716727_0_0_9; -.
DR OMA; WESQIDK; -.
DR EvolutionaryTrace; P0C0J1; -.
DR Proteomes; UP000000750; 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 3D-structure; Hydrolase; Methylation; Protease; Reference proteome;
KW Secreted; Signal; Thiol protease; Toxin; Virulence; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT PROPEP 28..145
FT /evidence="ECO:0000250"
FT /id="PRO_0000041939"
FT CHAIN 146..398
FT /note="Streptopain"
FT /id="PRO_0000041940"
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 VARIANT 8
FT /note="V -> I (in strain: 789)"
FT VARIANT 193
FT /note="V -> L (in strain: A-20)"
FT VARIANT 308
FT /note="G -> S (in strain: 789)"
FT MUTAGEN 334
FT /note="V->A: Reduces activity 130-fold."
FT /evidence="ECO:0000269|PubMed:19237546"
FT MUTAGEN 357
FT /note="W->A: Reduces activity 280-fold."
FT /evidence="ECO:0000269|PubMed:19237546"
FT MUTAGEN 359
FT /note="W->A: Reduces activity 420-fold."
FT /evidence="ECO:0000269|PubMed:19237546"
FT MUTAGEN 384
FT /note="G->D: Reduces activity 14-fold."
FT /evidence="ECO:0000269|PubMed:19237546"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:2JTC"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2JTC"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2JTC"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2JTC"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:2JTC"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2JTC"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:2JTC"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:2JTC"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:2JTC"
FT HELIX 255..271
FT /evidence="ECO:0007829|PDB:2JTC"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2JTC"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:2JTC"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2JTC"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:2JTC"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:2JTC"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:2JTC"
FT STRAND 339..351
FT /evidence="ECO:0007829|PDB:2JTC"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:2JTC"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:2JTC"
FT STRAND 388..394
FT /evidence="ECO:0007829|PDB:2JTC"
SQ SEQUENCE 398 AA; 43130 MW; 4D60DB0B80D687B4 CRC64;
MNKKKLGVRL 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
SVHQINRGDF SKQDWEAQID KELSQNQPVY YQGVGKVGGH AFVIDGADGR NFYHVNWGWG
GVSDGFFRLD ALNPSALGTG GGAGGFNGYQ SAVVGIKP
