ID   SSPP_STAA8              Reviewed;         388 AA.
AC   Q2G2R8;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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; OrderedLocusNames=SAOUHSC_02127;
OS   Staphylococcus aureus (strain NCTC 8325).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
RA   Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC8325 genome.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 215-222, AND INDUCTION.
RX   PubMed=14702415; DOI=10.1099/mic.0.26634-0;
RA   Shaw L., Golonka E., Potempa J., Foster S.J.;
RT   "The role and regulation of the extracellular proteases of
RT   Staphylococcus aureus.";
RL   Microbiology 150:217-228(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   -!- INDUCTION: Expression occurs in a growth phase-dependent manner
CC       with optimal expression at post-exponential phase. Up-regulated by
CC       agr (accessory gene regulator) and repressed by sarA
CC       (staphylococcal accessory regulator) and sigmaB factor.
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; CP000253; ABD31176.1; -; Genomic_DNA.
DR   RefSeq; YP_500618.1; -.
DR   SMR; Q2G2R8; 216-388.
DR   GeneID; 3921198; -.
DR   GenomeReviews; CP000253_GR; SAOUHSC_02127.
DR   KEGG; sao:SAOUHSC_02127; -.
DR   HOGENOM; Q2G2R8; -.
DR   OMA; Q2G2R8; YTINVSS.
DR   BioCyc; SAUR93061:SAOUHSC_02127-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   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Hydrolase; Protease;
KW   Secreted; Signal; Thiol protease; Virulence; Zymogen.
FT   SIGNAL        1     25       Potential.
FT   PROPEP       26    214       By similarity.
FT                                /FTId=PRO_0000247954.
FT   CHAIN       215    388       Staphopain A.
FT                                /FTId=PRO_0000247955.
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;  44262 MW;  45D76DE341101F0D 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
     YTMSELLNAT YNTNKYHAEA VMRFLHPNLQ GQRFQFTGLT PREMIYFGQT QGRSPQLLNR
     MTTYNEVDNL TKNNKGIAVL GSRVESRNGM HAGHAMAVVG NAKLDNGQEV IIIWNPWDNG
     FMTQDAKNNV IPVSNGDHYR WYSSIYGY
//