ID   SSPA_STAAW              Reviewed;         327 AA.
AC   Q8NX98;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 43.
DE   RecName: Full=Glutamyl endopeptidase;
DE            EC=3.4.21.19;
DE   AltName: Full=Staphylococcal serine proteinase;
DE   AltName: Full=V8 protease;
DE   AltName: Full=V8 proteinase;
DE   AltName: Full=Endoproteinase Glu-C;
DE   Flags: Precursor;
GN   Name=sspA; OrderedLocusNames=MW0932;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-
CC       terminal side of aspartate and glutamate. Along with other
CC       extracellular proteases it is involved in colonization and
CC       infection of human tissues. Required for proteolytic maturation of
CC       thiol protease sspB and inactivation of sspC, an inhibitor of
CC       sspB. It is the most important protease for degradation of
CC       fibronectin-binding protein (FnBP) and surface protein A, which
CC       are involved in adherence to host cells. May also protect bacteria
CC       against host defense mechanism by cleaving the immunoglobulin
CC       classes IgG, IgA and IgM. May be involved in the stability of
CC       secreted lipases (By similarity).
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- PTM: Proteolytically cleaved by aureolysin (aur). This cleavage
CC       leads to the activation of sspA (By similarity).
CC   -!- MISCELLANEOUS: The cascade of activation of extracellular
CC       proteases proceeds from the metalloprotease aureolysin (aur),
CC       through sspA to sspB (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S1B family.
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DR   EMBL; BA000033; BAB94797.1; -; Genomic_DNA.
DR   RefSeq; NP_645749.1; -.
DR   HSSP; P09332; 1DT2.
DR   SMR; Q8NX98; 69-284.
DR   GeneID; 1003044; -.
DR   GenomeReviews; BA000033_GR; MW0932.
DR   KEGG; sam:MW0932; -.
DR   HOGENOM; Q8NX98; -.
DR   OMA; Q8NX98; EDINFAN.
DR   BioCyc; SAUR196620:MW0932-MON; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000126; Pept_S1B_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR008256; Peptidase_S1B.
DR   InterPro; IPR008353; Peptidase_S1B_tx.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR01774; EXFOLTOXIN.
DR   PRINTS; PR00839; V8PROTEASE.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   PROSITE; PS00672; V8_HIS; 1.
DR   PROSITE; PS00673; V8_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Protease; Repeat; Secreted;
KW   Serine protease; Signal; Virulence; Zymogen.
FT   SIGNAL        1     29       Potential.
FT   PROPEP       30     68       By similarity.
FT                                /FTId=PRO_0000026894.
FT   CHAIN        69    327       Glutamyl endopeptidase.
FT                                /FTId=PRO_0000026895.
FT   REPEAT      289    291       1.
FT   REPEAT      292    294       2.
FT   REPEAT      295    297       3.
FT   REPEAT      298    300       4.
FT   REPEAT      301    303       5.
FT   REPEAT      304    306       6.
FT   REPEAT      307    309       7.
FT   REPEAT      310    312       8.
FT   REPEAT      313    315       9.
FT   REGION      289    315       9 X 3 AA repeats of P-[DN]-N.
FT   ACT_SITE    119    119       Charge relay system (By similarity).
FT   ACT_SITE    161    161       Charge relay system (By similarity).
FT   ACT_SITE    237    237       Charge relay system (By similarity).
FT   SITE         68     69       Cleavage; by aureolysin (By similarity).
SQ   SEQUENCE   327 AA;  35319 MW;  3A26D9A138E65367 CRC64;
     MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QSQSSKQQTP KIQKGGNLKP
     LEQREHANVI LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLTNKHV
     VDATHGDPHA LKAFPSAINQ DNYPNGGFTA EQITKYSGEG DLAIVKFSPN EQNKHIGEVV
     KPATMSNNAE TQVNQNITVT GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP
     VFNEKNEVIG IHWGGVPNEF NGAVFINENV RNFLKQNIED IHFANDDQPN NPDNPDNPNN
     PDNPNNPNNP DNPDNGDNNN SDNPDAA
//