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

 SPEB_STRPY              Reviewed;         398 AA.
P0C0J0; P00788; P26296; P68883; Q54960; Q54961; Q54962; Q54963;
Q54964; Q54965; Q54966; Q54967; Q54968; Q57024; Q57082; Q57202;
Q57211; Q57212; Q9S680;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-SEP-2005, sequence version 1.
31-JAN-2018, 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;
Streptococcus pyogenes.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=1314;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-32 AND
146-162.
STRAIN=86-858, and NY-5;
PubMed=2198264; DOI=10.1128/jb.172.8.4536-4542.1990;
Hauser A.R., Schlievert P.M.;
"Nucleotide sequence of the streptococcal pyrogenic exotoxin type B
gene and relationship between the toxin and the streptococcal
proteinase precursor.";
J. Bacteriol. 172:4536-4542(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
STRAIN=1226 / Serotype M44, 1233 / Serotype M17, 1289 / Serotype M5,
1294 / Serotype M19, 1590, 162 / Serotype M22, 165 / Serotype M,
168 / Serotype M66, 1719 / Serotype T8, 1832 / Serotype M76,
1838 / Serotype M27, 1841 / Serotype M41, 1842 / Serotype M43,
1864 / Serotype M56, 1870, 1871, 1872, 1882 / Serotype M59, 1893,
1896 / Serotype M10, 1898 / Serotype M15, 1901 / Serotype M23,
1911 / Serotype M75, 1914A, 1990 / Serotype M, 1991 / Serotype M,
2017 / Serotype M, 2018 / Serotype M, 262 / Serotype M,
282 / Serotype M12, 289 / Serotype T28, 302 / Serotype M73,
317 / Serotype M, 321 / Serotype M4, 327 / Serotype M2,
366 / Serotype M30, 427 / Serotype M31, 429 / Serotype M8,
650 / Serotype M11, 659 / Serotype M13, 660 / Serotype M14,
684 / Serotype M24, 686 / Serotype M25, 719 / Serotype M49,
758 / Serotype M75, 796 / Serotype M9, 800 / Serotype M9, and
807 / Serotype M33;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sv / Serotype M23;
Hong K.;
"A novel cloning method used arbitrarily primed PCR.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[4]
PRELIMINARY PROTEIN SEQUENCE OF 28-86 AND 121-398.
Yonaha K., Elliott S.D., Liu T.-Y.;
"Primary structure of zymogen of streptococcal proteinase.";
J. Protein Chem. 1:317-334(1982).
[5]
PRELIMINARY PROTEIN SEQUENCE OF 146-398.
PubMed=1270417;
Tai J.Y., Kortt A.A., Liu T.-Y., Elliott S.D.;
"Primary structure of streptococcal proteinase. III. Isolation of
cyanogen bromide peptides: complete covalent structure of the
polypeptide chain.";
J. Biol. Chem. 251:1955-1959(1976).
[6]
METHYLTHIOLATION AT CYS-192.
PubMed=6381494;
Lo S.S., Fraser B.A., Liu T.-Y.;
"The mixed disulfide in the zymogen of streptococcal proteinase.
Characterization and implication for its biosynthesis.";
J. Biol. Chem. 259:11041-11045(1984).
[7]
FUNCTION.
STRAIN=NZ131 / Serotype M49,T14;
PubMed=9864206;
Kuo C.-F., Wu J.-J., Tsai P.-J., Kao F.-J., Lei H.-Y., Lin M.T.,
Lin Y.-S.;
"Streptococcal pyrogenic exotoxin B induces apoptosis and reduces
phagocytic activity in U937 cells.";
Infect. Immun. 67:126-130(1999).
[8]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 28-398.
PubMed=10681429; DOI=10.1073/pnas.040549997;
Kagawa T.F., Cooney J.C., Baker H.M., McSweeney S., Liu M., Gubba S.,
Musser J.M., Baker E.N.;
"Crystal structure of the zymogen form of the group A Streptococcus
virulence factor SpeB: an integrin-binding cysteine protease.";
Proc. Natl. Acad. Sci. U.S.A. 97:2235-2240(2000).
[9]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 146-398 IN COMPLEX WITH THE
SYNTHETIC INHIBITOR E64, ACTIVE SITE, AND SUBUNIT.
PubMed=19712682; DOI=10.1016/j.jmb.2009.08.046;
Olsen J.G., Dagil R., Niclasen L.M., Sorensen O.E., Kragelund B.B.;
"Structure of the mature Streptococcal cysteine protease exotoxin
mSpeB in its active dimeric form.";
J. Mol. Biol. 393:693-703(2009).
-!- 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. {ECO:0000269|PubMed:9864206}.
-!- CATALYTIC ACTIVITY: Preferential cleavage with hydrophobic
residues at P2, P1 and P1'.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19712682}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the peptidase C10 family. {ECO:0000305}.
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EMBL; M86905; AAA26978.1; -; Genomic_DNA.
EMBL; L26126; AAA26992.1; -; Genomic_DNA.
EMBL; L26127; AAA26993.1; -; Genomic_DNA.
EMBL; L26128; AAA26994.1; -; Genomic_DNA.
EMBL; L26129; AAA26995.1; -; Genomic_DNA.
EMBL; L26130; AAA26996.1; -; Genomic_DNA.
EMBL; L26131; AAA26997.1; -; Genomic_DNA.
EMBL; L26132; AAA26998.1; -; Genomic_DNA.
EMBL; L26133; AAA26999.1; -; Genomic_DNA.
EMBL; L26135; AAA27001.1; -; Genomic_DNA.
EMBL; L26136; AAA27002.1; -; Genomic_DNA.
EMBL; L26137; AAA27003.1; -; Genomic_DNA.
EMBL; L26138; AAA27004.1; -; Genomic_DNA.
EMBL; L26139; AAA27005.1; -; Genomic_DNA.
EMBL; L26140; AAA27006.1; -; Genomic_DNA.
EMBL; L26141; AAA27007.1; -; Genomic_DNA.
EMBL; L26142; AAA27008.1; -; Genomic_DNA.
EMBL; L26143; AAA27009.1; -; Genomic_DNA.
EMBL; L26144; AAA27010.1; -; Genomic_DNA.
EMBL; L26145; AAA27011.1; -; Genomic_DNA.
EMBL; L26147; AAA27013.1; -; Genomic_DNA.
EMBL; L26148; AAA27014.1; -; Genomic_DNA.
EMBL; L26149; AAA27015.1; -; Genomic_DNA.
EMBL; L26150; AAA27016.1; -; Genomic_DNA.
EMBL; L26151; AAA26980.1; -; Genomic_DNA.
EMBL; L26152; AAA26981.1; -; Genomic_DNA.
EMBL; L26153; AAA26982.1; -; Genomic_DNA.
EMBL; L26154; AAA26983.1; -; Genomic_DNA.
EMBL; L26155; AAA26984.1; -; Genomic_DNA.
EMBL; L26156; AAA26985.1; -; Genomic_DNA.
EMBL; L26157; AAA26986.1; -; Genomic_DNA.
EMBL; L26159; AAA26988.1; -; Genomic_DNA.
EMBL; L26160; AAA26989.1; -; Genomic_DNA.
EMBL; L26161; AAA26990.1; -; Genomic_DNA.
EMBL; L26162; AAA26991.1; -; Genomic_DNA.
EMBL; AB030578; BAB16027.1; -; Genomic_DNA.
PIR; A37768; A37768.
RefSeq; WP_002991253.1; NZ_NJPV01000004.1.
RefSeq; WP_009881074.1; NZ_CP022354.1.
RefSeq; WP_011285235.1; NZ_FNML01000023.1.
RefSeq; WP_014407896.1; NZ_MSMN01000001.1.
RefSeq; WP_021733538.1; NZ_NBYU01000012.1.
RefSeq; WP_023611203.1; NZ_CP014278.2.
RefSeq; WP_031488619.1; NZ_NBYT01000005.1.
RefSeq; WP_038433740.1; NZ_CP008695.1.
RefSeq; WP_076639504.1; NZ_FNMQ01000011.1.
PDB; 1DKI; X-ray; 1.60 A; A/B/C/D=28-398.
PDB; 1PVJ; X-ray; 3.00 A; A/B/C/D=31-398.
PDB; 2UZJ; X-ray; 1.55 A; A/B=146-398.
PDBsum; 1DKI; -.
PDBsum; 1PVJ; -.
PDBsum; 2UZJ; -.
ProteinModelPortal; P0C0J0; -.
SMR; P0C0J0; -.
BindingDB; P0C0J0; -.
ChEMBL; CHEMBL2034806; -.
DrugBank; DB02766; (3r)-3-{[(Benzyloxy)Carbonyl]Amino}-2-Oxo-4-Phenylbutane-1-Diazonium.
eggNOG; ENOG4105JBQ; Bacteria.
eggNOG; ENOG4111S8V; LUCA.
BRENDA; 3.4.22.10; 5935.
SABIO-RK; P0C0J0; -.
EvolutionaryTrace; P0C0J0; -.
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.
GO; GO:0035897; P:proteolysis in other organism; IMP:CACAO.
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;
3D-structure; Direct protein sequencing; Hydrolase; Methylation;
Protease; Secreted; Signal; Thiol protease; Toxin; Virulence; Zymogen.
SIGNAL 1 27 {ECO:0000269|PubMed:2198264}.
PROPEP 28 145 {ECO:0000269|PubMed:2198264}.
/FTId=PRO_0000028503.
CHAIN 146 398 Streptopain.
/FTId=PRO_0000028504.
ACT_SITE 192 192 Nucleophile.
{ECO:0000269|PubMed:19712682}.
ACT_SITE 340 340 Proton acceptor.
{ECO:0000269|PubMed:19712682}.
MOD_RES 192 192 Cysteine methyl disulfide; in zymogen
form. {ECO:0000269|PubMed:6381494}.
VARIANT 17 17 G -> S (in strain: MGAS 1896).
VARIANT 80 80 V -> I (in strain: MGAS 168).
VARIANT 111 111 A -> V (in strain: MGAS 165, 168, 429,
659, 660, 796, 800, 1719, 1838, 1882,
2017 and 2018).
VARIANT 137 137 T -> I (in strain: MGAS 650).
VARIANT 154 154 D -> N (in strain: MGAS 684).
VARIANT 211 211 L -> V (in strain: MGAS 366, 427, 758,
1294, 1911, 1914A and 1991).
VARIANT 305 305 I -> V (in strain: MGAS 1901 and Sv).
VARIANT 308 308 S -> G (in strain: MGAS 429, 659, 807,
1226, 1719, 1832, 1842, 1871, 1872, 2017
and 2018).
VARIANT 317 317 A -> S (in strain: MGAS 165, 168, 289,
302, 1233 and 1898).
VARIANT 384 384 G -> D (in strain: MGAS 1871).
VARIANT 394 394 V -> I (in strain: MGAS 366 and 1294).
CONFLICT 84 85 ST -> AS (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 169 169 L -> I (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 187 191 HAATG -> AATGH (in Ref. 4; AA sequence
and 5; AA sequence). {ECO:0000305}.
CONFLICT 208 208 N -> D (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 213 213 D -> N (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 222 223 NP -> PD (in Ref. 4; AA sequence and 5;
AA sequence). {ECO:0000305}.
CONFLICT 226 226 N -> D (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 241 241 N -> D (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 253 257 ESNVQ -> QSQNV (in Ref. 4; AA sequence
and 5; AA sequence). {ECO:0000305}.
CONFLICT 306 306 N -> D (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 332 332 Q -> E (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 346 348 GAD -> DGA (in Ref. 4; AA sequence and 5;
AA sequence). {ECO:0000305}.
CONFLICT 356 356 N -> D (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 390 390 Q -> E (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
HELIX 35 38 {ECO:0000244|PDB:1DKI}.
HELIX 40 47 {ECO:0000244|PDB:1DKI}.
STRAND 64 66 {ECO:0000244|PDB:1PVJ}.
TURN 71 73 {ECO:0000244|PDB:1PVJ}.
STRAND 75 82 {ECO:0000244|PDB:1DKI}.
STRAND 84 86 {ECO:0000244|PDB:1DKI}.
STRAND 88 93 {ECO:0000244|PDB:1DKI}.
STRAND 99 107 {ECO:0000244|PDB:1DKI}.
HELIX 115 130 {ECO:0000244|PDB:1DKI}.
HELIX 131 133 {ECO:0000244|PDB:1DKI}.
HELIX 152 155 {ECO:0000244|PDB:2UZJ}.
TURN 164 169 {ECO:0000244|PDB:2UZJ}.
HELIX 192 204 {ECO:0000244|PDB:2UZJ}.
STRAND 214 217 {ECO:0000244|PDB:2UZJ}.
STRAND 230 233 {ECO:0000244|PDB:2UZJ}.
HELIX 235 237 {ECO:0000244|PDB:2UZJ}.
TURN 242 244 {ECO:0000244|PDB:2UZJ}.
HELIX 255 271 {ECO:0000244|PDB:2UZJ}.
STRAND 277 279 {ECO:0000244|PDB:2UZJ}.
HELIX 285 294 {ECO:0000244|PDB:2UZJ}.
STRAND 303 306 {ECO:0000244|PDB:2UZJ}.
HELIX 307 309 {ECO:0000244|PDB:2UZJ}.
HELIX 312 324 {ECO:0000244|PDB:2UZJ}.
STRAND 329 335 {ECO:0000244|PDB:2UZJ}.
STRAND 338 351 {ECO:0000244|PDB:2UZJ}.
STRAND 353 356 {ECO:0000244|PDB:2UZJ}.
TURN 360 363 {ECO:0000244|PDB:2UZJ}.
STRAND 365 368 {ECO:0000244|PDB:2UZJ}.
HELIX 375 377 {ECO:0000244|PDB:2UZJ}.
STRAND 388 394 {ECO:0000244|PDB:2UZJ}.
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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