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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(02)08713-5; PubMed=12044378 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T.,
Takeuchi F.,
Kuroda M.,
Yuzawa H.,
Aoki K.,
Oguchi A.,
Nagai Y.,
Iwama N.,
Asano K.,
Naimi T.,
Kuroda H.,
Cui L.,
Yamamoto K.,
Hiramatsu K.;
"Genome and virulence determinants of high virulence community-acquired MRSA.";
Lancet 359:1819-1827(2002).
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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: 327 AA [This is the length of the unprocessed precursor] |
Molecular weight: 35319 Da [This is the MW of the unprocessed precursor] |
CRC64: 3A26D9A138E65367 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QSQSSKQQTP 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
PDNPNNPNNP DNPDNGDNNN SDNPDAA
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Q8NX98 in FASTA format |
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ExPASy Home page
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