ID   SSPP_STAAM              Reviewed;         388 AA.
AC   P65825; Q99SX8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=SAV1909;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158878;
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: 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; BA000017; BAB58071.1; -; Genomic_DNA.
DR   RefSeq; NP_372433.1; -.
DR   HSSP; P81297; 1CV8.
DR   SMR; P65825; 216-388.
DR   GeneID; 1121922; -.
DR   GenomeReviews; BA000017_GR; SAV1909.
DR   KEGG; sav:SAV1909; -.
DR   HOGENOM; P65825; -.
DR   OMA; P65825; YTINVSS.
DR   BioCyc; SAUR158878:SAV1909-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_0000026549.
FT   CHAIN       215    388       Staphopain A.
FT                                /FTId=PRO_0000026550.
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;  44204 MW;  08540023411772CF CRC64;
     MKRNFPKLIA LSLIFSLSVT PIANAESNSN IKAKDKKHVQ VNVEDKSVPT DVRNLAQKDY
     LSYVTSLDKI YNKEKASYTL GEPFKIYKFN KKSDGNYYFP VLNTEGNIDY IVTISPKITK
     YSSSSSKYTI NVSPFLSKVL NQYKDQQITI LTNSKGYYVV TQNHKAKLVL KTPRLEDKKL
     KKTESIPTGN NVTQLKQKAS VTMPTSQFKS NNYTYNEQYI NKLENFKIRE TQGNNGWCAG
     YTMSALLNAT YNTNKYHAEA VMRFLHPNLQ GQRFQFTGLT PREMIYFGQT QGRSPQLLNR
     MTTYNEVDNL TKNNKGIAVL GSRVESRNGM HAGHAMAVVG NAKLDNGQEV IIIWNPWDNG
     FMTQDAKNNV IPVSNGDHYR WYSSIYGY
//