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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0402521101; PubMed=15213324 [NCBI, ExPASy, EBI, Israel, Japan]
Holden M.T.G.,
Feil E.J.,
Lindsay J.A.,
Peacock S.J.,
Day N.P.J.,
Enright M.C.,
Foster T.J.,
Moore C.E.,
Hurst L.,
Atkin R.,
Barron A.,
Bason N.,
Bentley S.D.,
Chillingworth C.,
Chillingworth T.,
Churcher C.,
Clark L.,
Corton C.,
Cronin A., ![]()
Doggett J.,
Dowd L.,
Feltwell T.,
Hance Z.,
Harris B.,
Hauser H.,
Holroyd S.,
Jagels K.,
James K.D.,
Lennard N.,
Line A.,
Mayes R.,
Moule S.,
Mungall K.,
Ormond D.,
Quail M.A.,
Rabbinowitsch E.,
Rutherford K.M.,
Sanders M.,
Sharp S.,
Simmonds M.,
Stevens K.,
Whitehead S.,
Barrell B.G.,
Spratt B.G.,
Parkhill J.;
"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance.";
Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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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 (By similarity).
- CATALYTIC ACTIVITY: Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
- SUBCELLULAR LOCATION: Secreted (By similarity).
- PTM: Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of sspA (By similarity).
- MISCELLANEOUS: The cascade of activation of extracellular proteases proceeds from the metalloprotease aureolysin (aur), through sspA to sspB (By similarity).
- SIMILARITY: Belongs to the peptidase S1B family [view classification].
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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: 357 AA [This is the length of the unprocessed precursor] |
Molecular weight: 38639 Da [This is the MW of the unprocessed precursor] |
CRC64: 0AB1A85D162A0395 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQTDKQQTP KIQKGGNLKP
70 80 90 100 110 120
LEQRERANVI LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLTNKHI
130 140 150 160 170 180
VDATHGDPHA LKAFASAINQ DNYPNGGFTA EQITKYSGEG DLAIVKFSPN EQNKHIGEVV
190 200 210 220 230 240
KPATMSNNAE TQVNQNITVT GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP
250 260 270 280 290 300
VFNEKNEVIG IHWGGVPNQF NGAVFINENV RNFLKQNIED INFANDDHPN NPDNPDNPNN
310 320 330 340 350
PDNPNNPDNP NNPDNPDNPN NPDNPNNPDN PNNPDQPNNP NNPDNGDNNN SDNPDAA
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Q6GI34 in FASTA format |
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ExPASy Home page
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