ID   SSPA_STAAN              Reviewed;         342 AA.
AC   Q7A6A6;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 35.
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=SA0901;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA   Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000018; BAB42146.1; -; Genomic_DNA.
DR   PIR; G89873; G89873.
DR   RefSeq; NP_374168.1; -.
DR   SMR; Q7A6A6; 69-284.
DR   GeneID; 1123724; -.
DR   GenomeReviews; BA000018_GR; SA0901.
DR   KEGG; sau:SA0901; -.
DR   HOGENOM; Q7A6A6; -.
DR   OMA; Q7A6A6; EDINFAN.
DR   BioCyc; SAUR158879:SA0901-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_0000026888.
FT   CHAIN        69    342       Glutamyl endopeptidase.
FT                                /FTId=PRO_0000026889.
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      316    318       9.
FT   REPEAT      319    321       10.
FT   REPEAT      322    324       11.
FT   REPEAT      325    327       12.
FT   REPEAT      328    330       13.
FT   REGION      289    330       13 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   342 AA;  36977 MW;  5AEF42DCE01C4B24 CRC64;
     MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQSSKQQTP KIKKGGNLKP
     LEQREHANVI LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLTNKHV
     VDATHGDPHA LKAFPSAINQ DNYPNGGFTA EQITKYSGEG DLAIVKFSPN EQNKHIGEVV
     KPATMSNNAE TQVNQNITVT GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP
     VFNEKNEVIG IHWGGVPNEF NGAVFINENV RNFLKQNIED IHFANDDQPN NPDNPDNPNN
     PDNPNNPDNP NNPDEPNNPD NPNNPDNPDN GDNNNSDNPD AA
//