ID   SSPP_STAAR              Reviewed;         388 AA.
AC   Q6GFE8;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Staphopain A;
DE            EC=3.4.22.48;
DE   AltName: Full=Staphylopain A;
DE   AltName: Full=Staphylococcal cysteine proteinase A;
DE   Flags: Precursor;
GN   Name=sspP; Synonyms=scpA; OrderedLocusNames=SAR2001;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Cysteine protease able to degrade elastin (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Broad endopeptidase action on proteins
CC       including elastin, but rather limited hydrolysis of small-molecule
CC       substrates. Assays are conveniently made with hemoglobin, casein
CC       or Z-Phe-Arg-NHMec as substrate.
CC   -!- ENZYME REGULATION: Prematurely activated/folded staphopain A is
CC       inhibited by staphostatin A (scpB), which is probably required to
CC       protect staphylococcal cytoplasmic proteins from degradation by
CC       scpA (By similarity).
CC   -!- SUBUNIT: In the cytoplasm, prematurely activated/folded scpA forms
CC       a stable non-covalent complex with scpB (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- PTM: Cleavage leads to the activation of scpA probably by an auto-
CC       catalytic manner (By similarity).
CC   -!- MISCELLANEOUS: The catalytic maturation of scpA appears to reside
CC       outside the cascade of activation started by the metalloprotease
CC       aureolysin (aur) (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C47 family.
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DR   EMBL; BX571856; CAG40986.1; -; Genomic_DNA.
DR   RefSeq; YP_041374.1; -.
DR   SMR; Q6GFE8; 216-388.
DR   GeneID; 2859733; -.
DR   GenomeReviews; BX571856_GR; SAR2001.
DR   KEGG; sar:SAR2001; -.
DR   HOGENOM; Q6GFE8; -.
DR   OMA; Q6GFE8; YTINVSS.
DR   BioCyc; SAUR282458:SAR2001-MON; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR008750; Peptidase_C47.
DR   Pfam; PF05543; Peptidase_C47; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; FALSE_NEG.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; FALSE_NEG.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Protease; Secreted; Signal;
KW   Thiol protease; Virulence; Zymogen.
FT   SIGNAL        1     25       Potential.
FT   PROPEP       26    214       By similarity.
FT                                /FTId=PRO_0000026553.
FT   CHAIN       215    388       Staphopain A.
FT                                /FTId=PRO_0000026554.
FT   ACT_SITE    238    238       By similarity.
FT   ACT_SITE    334    334       By similarity.
FT   ACT_SITE    355    355       By similarity.
FT   SITE        214    215       Cleavage (By similarity).
SQ   SEQUENCE   388 AA;  44048 MW;  44017EA70E289F14 CRC64;
     MKRNFPKLIA LSLIFSLSIT PIANAESNSN IKAKDKRHVQ VNVEDKSVPT DVRNLAQKDY
     LSYVTSLDKI YNKEKASYTL GEPFKIYKFN KKSDGNYYFP VLNTEGNIDY IVTISPKVTK
     DSSSSSKYTI NVSSFLSKAL NEYKDQQITI LTNSKGYYVV TQNHKAKLVL KTPRLEDKKA
     KKTESIPTGN NVTQLKQKAS VTMPTSQFKS NNYTYNEQYV NKLENFKIRE TQGNNGWCAG
     YTMSALLNAT YNTNKYHAEA VMRFLHPNLQ GQQFQFTGLT PREMIYFGQT QGRSPQLLNR
     MTTYNEVDNL TKNNKGIAIL GSRVESRNGM HAGHAMAVVG NAKLNNGQEV IIIWNPWDNG
     FMTQDAKNNV IPVSNGDHYQ WYSSIYGY
//