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Reviewed, UniProtKB/Swiss-Prot P0C0J0 (SPEB_STRPY)

Last modified June 16, 2009. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Streptopain
    EC=3.4.22.10
Alternative name(s):
    Streptococcal cysteine proteinase
    Streptococcus peptidase A
      Short name=SPP
    Exotoxin type B
    SPE B
Gene names
Name: speB
OrganismStreptococcus pyogenes
Taxonomic identifier1314 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

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. Ref.7

Catalytic activity

Preferential cleavage with hydrophobic residues at P2, P1 and P1'.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase C10 family.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
Toxin
   PTMMethylation
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.1 Ref.4
Propeptide28 – 145118 Ref.5
PRO_0000028503
Chain146 – 398253Streptopain
PRO_0000028504

Sites

Active site1921
Active site3401

Amino acid modifications

Modified residue1921Cysteine methyl disulfide; in zymogen form

Natural variations

Natural variant171G → S in strain: MGAS 1896.
Natural variant801V → I in strain: MGAS 168.
Natural variant1111A → V in strain: MGAS 165, 168, 429, 659, 660, 796, 800, 1719, 1838, 1882, 2017 and 2018.
Natural variant1371T → I in strain: MGAS 650.
Natural variant1541D → N in strain: MGAS 684.
Natural variant2111L → V in strain: MGAS 366, 427, 758, 1294, 1911, 1914A and 1991.
Natural variant3051I → V in strain: MGAS 1901 and Sv.
Natural variant3081S → G in strain: MGAS 429, 659, 807, 1226, 1719, 1832, 1842, 1871, 1872, 2017 and 2018.
Natural variant3171A → S in strain: MGAS 165, 168, 289, 302, 1233 and 1898.
Natural variant3841G → D in strain: MGAS 1871.
Natural variant3941V → I in strain: MGAS 366 and 1294.

Experimental info

Sequence conflict84 – 852ST → AS AA sequence Ref.4
Sequence conflict1691L → I AA sequence Ref.4
Sequence conflict187 – 1915HAATG → AATGH AA sequence Ref.4
Sequence conflict187 – 1915HAATG → AATGH AA sequence Ref.5
Sequence conflict2081N → D AA sequence Ref.4
Sequence conflict2081N → D AA sequence Ref.5
Sequence conflict2131D → N AA sequence Ref.4
Sequence conflict2131D → N AA sequence Ref.5
Sequence conflict222 – 2232NP → PD AA sequence Ref.4
Sequence conflict222 – 2232NP → PD AA sequence Ref.5
Sequence conflict2261N → D AA sequence Ref.4
Sequence conflict2261N → D AA sequence Ref.5
Sequence conflict2411N → D AA sequence Ref.4
Sequence conflict2411N → D AA sequence Ref.5
Sequence conflict253 – 2575ESNVQ → QSQNV Ref.4
Sequence conflict253 – 2575ESNVQ → QSQNV AA sequence Ref.5
Sequence conflict3061N → D AA sequence; AA sequence Ref.4
Sequence conflict3321Q → E AA sequence Ref.4
Sequence conflict3321Q → E AA sequence Ref.5
Sequence conflict346 – 3483GAD → DGA AA sequence Ref.4
Sequence conflict346 – 3483GAD → DGA AA sequence Ref.5
Sequence conflict3561N → D AA sequence Ref.4
Sequence conflict3561N → D AA sequence Ref.5
Sequence conflict3901Q → E AA sequence Ref.4
Sequence conflict3901Q → E AA sequence Ref.5

Secondary structure

........................................................ 398
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C0J0-1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 16FF180D720AEE0F

FASTA39843,174
        10         20         30         40         50         60 
MNKKKLGIRL LSLLALGGFV LANPVFADQN FARNEKEAKD SAITFIQKSA AIKAGARSAE 

        70         80         90        100        110        120 
DIKLDKVNLG GELSGSNMYV YNISTGGFVI VSGDKRSPEI LGYSTSGSFD ANGKENIASF 

       130        140        150        160        170        180 
MESYVEQIKE NKKLDTTYAG TAEIKQPVVK SLLDSKGIHY NQGNPYNLLT PVIEKVKPGE 

       190        200        210        220        230        240 
QSFVGQHAAT GCVATATAQI MKYHNYPNKG LKDYTYTLSS NNPYFNHPKN LFAAISTRQY 

       250        260        270        280        290        300 
NWNNILPTYS GRESNVQKMA ISELMADVGI SVDMDYGPSS GSAGSSRVQR ALKENFGYNQ 

       310        320        330        340        350        360 
SVHQINRSDF SKQDWEAQID KELSQNQPVY YQGVGKVGGH AFVIDGADGR NFYHVNWGWG 

       370        380        390 
GVSDGFFRLD ALNPSALGTG GGAGGFNGYQ SAVVGIKP 

« Hide

References

[1]"Nucleotide sequence of the streptococcal pyrogenic exotoxin type B gene and relationship between the toxin and the streptococcal proteinase precursor."
Hauser A.R., Schlievert P.M.
J. Bacteriol. 172:4536-4542(1990) [PubMed: 2198264] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-32 AND 146-162.
Strain: 86-858 and NY-5.
[2]"A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin."
Kapur V., Topouzis S., Majesky M.W., Li L.L., Hamrick M.R., Hamill R.J., Patti J.M., Musser J.M.
Microb. Pathog. 15:327-346(1993) [PubMed: 7516997] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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.
[3]"A novel cloning method used arbitrarily primed PCR."
Hong K.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sv / Serotype M23.
[4]"Primary structure of zymogen of streptococcal proteinase."
Yonaha K., Elliott S.D., Liu T.-Y.
J. Protein Chem. 1:317-334(1982)
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 28-86 AND 121-398.
[5]"Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain."
Tai J.Y., Kortt A.A., Liu T.-Y., Elliott S.D.
J. Biol. Chem. 251:1955-1959(1976) [PubMed: 1270417] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 146-398.
[6]"The mixed disulfide in the zymogen of streptococcal proteinase. Characterization and implication for its biosynthesis."
Lo S.S., Fraser B.A., Liu T.-Y.
J. Biol. Chem. 259:11041-11045(1984) [PubMed: 6381494] [Abstract]
Cited for: CYSTEINE METHYL DISULFIDE.
[7]"Streptococcal pyrogenic exotoxin B induces apoptosis and reduces phagocytic activity in U937 cells."
Kuo C.-F., Wu J.-J., Tsai P.-J., Kao F.-J., Lei H.-Y., Lin M.T., Lin Y.-S.
Infect. Immun. 67:126-130(1999) [PubMed: 9864206] [Abstract]
Cited for: FUNCTION.
Strain: NZ131 / Serotype M49,T14.
+Additional computationally mapped references.

Cross-references

Sequence databases

M86905 Genomic DNA. Translation: AAA26978.1.
L26126 Genomic DNA. Translation: AAA26992.1.
L26127 Genomic DNA. Translation: AAA26993.1.
L26128 Genomic DNA. Translation: AAA26994.1.
L26129 Genomic DNA. Translation: AAA26995.1.
L26130 Genomic DNA. Translation: AAA26996.1.
L26131 Genomic DNA. Translation: AAA26997.1.
L26132 Genomic DNA. Translation: AAA26998.1.
L26133 Genomic DNA. Translation: AAA26999.1.
L26135 Genomic DNA. Translation: AAA27001.1.
L26136 Genomic DNA. Translation: AAA27002.1.
L26137 Genomic DNA. Translation: AAA27003.1.
L26138 Genomic DNA. Translation: AAA27004.1.
L26139 Genomic DNA. Translation: AAA27005.1.
L26140 Genomic DNA. Translation: AAA27006.1.
L26141 Genomic DNA. Translation: AAA27007.1.
L26142 Genomic DNA. Translation: AAA27008.1.
L26143 Genomic DNA. Translation: AAA27009.1.
L26144 Genomic DNA. Translation: AAA27010.1.
L26145 Genomic DNA. Translation: AAA27011.1.
L26147 Genomic DNA. Translation: AAA27013.1.
L26148 Genomic DNA. Translation: AAA27014.1.
L26149 Genomic DNA. Translation: AAA27015.1.
L26150 Genomic DNA. Translation: AAA27016.1.
L26151 Genomic DNA. Translation: AAA26980.1.
L26152 Genomic DNA. Translation: AAA26981.1.
L26153 Genomic DNA. Translation: AAA26982.1.
L26154 Genomic DNA. Translation: AAA26983.1.
L26155 Genomic DNA. Translation: AAA26984.1.
L26156 Genomic DNA. Translation: AAA26985.1.
L26157 Genomic DNA. Translation: AAA26986.1.
L26159 Genomic DNA. Translation: AAA26988.1.
L26160 Genomic DNA. Translation: AAA26989.1.
L26161 Genomic DNA. Translation: AAA26990.1.
L26162 Genomic DNA. Translation: AAA26991.1.
AB030578 Genomic DNA. Translation: BAB16027.1.
PIRA37768.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DKIX-ray1.60A/B/C/D28-398[»]
1PVJX-ray3.00A/B/C/D31-398[»]
ModBaseSearch...

Protein family/group databases

MEROPSC10.001.

Enzyme and pathway databases

BRENDA3.4.22.10. 701.

Family and domain databases

InterProIPR000200. Peptidase_C10.
[Graphical view]
PfamPF01640. Peptidase_C10. 1 hit.
[Graphical view]
PRINTSPR00797. STREPTOPAIN.
ProDomPD004169. Peptidase_C10. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameSPEB_STRPY
AccessionPrimary (citable) accession number: P0C0J0
Secondary accession number(s): P00788 expand/collapse secondary AC list , P26296, P68883, Q54960, Q54961, Q54962, Q54963, Q54964, Q54965, Q54966, Q54967, Q54968, Q57024, Q57082, Q57202, Q57211, Q57212, Q9S680
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 13, 2005
Last modified: June 16, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents