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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 27733 / V8;
DOI=10.1093/nar/15.16.6757; PubMed=3306605 [NCBI, ExPASy, EBI, Israel, Japan]
Carmona C.,
Gray G.L.;
"Nucleotide sequence of the serine protease gene of Staphylococcus aureus, strain V8.";
Nucleic Acids Res. 15:6757-6757(1987).
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[2]
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PROTEIN SEQUENCE OF 69-280.
STRAIN=ATCC 27733 / V8;
PubMed=96922 [NCBI, ExPASy, EBI, Israel, Japan]
Drapeau G.R.;
"The primary structure of staphylococcal protease.";
Can. J. Biochem. 56:534-544(1978).
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[3]
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FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 27733 / V8;
PubMed=4627743 [NCBI, ExPASy, EBI, Israel, Japan]
Drapeau G.R.,
Boily Y.,
Houmard J.;
"Purification and properties of an extracellular protease of Staphylococcus aureus.";
J. Biol. Chem. 247:6720-6726(1972).
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[4]
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FUNCTION.
STRAIN=ATCC 27733 / V8;
DOI=10.1016/0165-2478(92)90124-7; PubMed=1372285 [NCBI, ExPASy, EBI, Israel, Japan]
Prokesova L.,
Potuznikova B.,
Potempa J.,
Zikan J.,
Radl J.,
Hachova L.,
Baran K.,
Porwit-Bobr Z.,
John C.;
"Cleavage of human immunoglobulins by serine proteinase from Staphylococcus aureus.";
Immunol. Lett. 31:259-265(1992).
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[5]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 69-336.
STRAIN=ATCC 27733 / V8;
Yamada K.,
Ohta M.,
Hasegawa T.,
Torii K.,
Murakami M.,
Kouyama K.;
"Crystal structure of an alkaline form of V8 protease from Staphylococcus aureus.";
Submitted (JUN-2004) to the PDB data bank.
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- FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease sspB and inactivation of sspC, an inhibitor of sspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases.
- CATALYTIC ACTIVITY: Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
- SUBCELLULAR LOCATION: Secreted.
- PTM: Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of sspA.
- MISCELLANEOUS: The cascade of activation of extracellular proteases proceeds from the metalloprotease aureolysin (aur), through sspA to sspB.
- SIMILARITY: Belongs to the peptidase S1B family [view classification].
- WEB RESOURCE: Name=Worthington enzyme manual; URL="http://www.worthington-biochem.com/STAP/";.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 336 AA [This is the length of the unprocessed precursor] |
Molecular weight: 36326 Da [This is the MW of the unprocessed precursor] |
CRC64: 8B138D0C7996AA3E [This is a checksum on the sequence] |
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10 20 30 40 50 60
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQSSKQQTP KIQKGGNLKP
70 80 90 100 110 120
LEQREHANVI LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLTNKHV
130 140 150 160 170 180
VDATHGDPHA LKAFPSAINQ DNYPNGGFTA EQITKYSGEG DLAIVKFSPN EQNKHIGEVV
190 200 210 220 230 240
KPATMSNNAE TQVNQNITVT GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP
250 260 270 280 290 300
VFNEKNEVIG IHWGGVPNEF NGAVFINENV RNFLKQNIED IHFANDDQPN NPDNPDNPNN
310 320 330
PDNPNNPDEP NNPDNPNNPD NPDNGDNNNS DNPDAA
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P0C1U8 in FASTA format |
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ExPASy Home page
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