ID   ECPA_STAEP              Reviewed;         174 AA.
AC   P0C0P9; Q8CMM9; Q9EWC9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Extracellular cysteine protease;
DE            EC=3.4.22.-;
DE   AltName: Full=Staphopain;
GN   Name=ecpA; Synonyms=ecp;
OS   Staphylococcus epidermidis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-47 AND 149-174,
RP   FUNCTION, AND ACTIVITY REGULATION.
RC   STRAIN=6746;
RX   PubMed=11767947; DOI=10.1515/bc.2001.192;
RA   Dubin G., Chmiel D., Mak P., Rakwalska M., Rzychon M., Dubin A.;
RT   "Molecular cloning and biochemical characterisation of proteases from
RT   Staphylcoccus epidermidis.";
RL   Biol. Chem. 382:1575-1582(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-12, FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 14990 / DSM 20044 / CIP 81.55 / NCTC 11047, TU 3298 / DSM 3095,
RC   and TU 9142;
RX   PubMed=15255185; DOI=10.1515/bc.2004.062;
RA   Oleksy A., Golonka E., Banbula A., Szmyd G., Moon J., Kubica M.,
RA   Greenbaum D., Bogyo M., Foster T.J., Travis J., Potempa J.;
RT   "Growth phase-dependent production of a cell wall-associated elastinolytic
RT   cysteine proteinase by Staphylococcus epidermidis.";
RL   Biol. Chem. 385:525-535(2004).
CC   -!- FUNCTION: Cysteine protease able to cleave elastin, insulin, myoglobin,
CC       fibronectin, fibrinogen, HMW-kininogen, alpha-1-protease inhibitor and
CC       alpha-1-antitrypsin. Along with other extracellular proteases may
CC       contribute to the colonization and infection of human tissues.
CC       {ECO:0000269|PubMed:11767947, ECO:0000269|PubMed:15255185}.
CC   -!- ACTIVITY REGULATION: Inhibited by heavy metal ions such as Zn(2+) or
CC       Ni(2+), iodoacetamide, N-ethylmaleimide, leupeptin, SDS and E-64. Also
CC       inhibited by chloromethylketones TPCK and TLCK and by human plasma
CC       inhibitor alpha-2-macroglobulin. Stimulated by L-cysteine.
CC       {ECO:0000269|PubMed:11767947}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0 for elastin hydrolysis.;
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:15255185}. Secreted {ECO:0000269|PubMed:15255185}.
CC   -!- INDUCTION: Expression occurs in a growth-phase-dependent manner with
CC       optimal expression at post-exponential phase.
CC       {ECO:0000269|PubMed:15255185}.
CC   -!- PTM: Proteolytically cleaved.
CC   -!- SIMILARITY: Belongs to the peptidase C47 family. {ECO:0000305}.
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DR   EMBL; AJ298299; CAC22343.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C0P9; -.
DR   SMR; P0C0P9; -.
DR   MEROPS; C47.003; -.
DR   KEGG; ag:CAC22343; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR008750; Peptidase_C47.
DR   Pfam; PF05543; Peptidase_C47; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Direct protein sequencing; Hydrolase; Protease; Secreted;
KW   Thiol protease; Virulence; Zymogen.
FT   CHAIN           1..174
FT                   /note="Extracellular cysteine protease"
FT                   /id="PRO_0000220334"
FT   ACT_SITE        24
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
SQ   SEQUENCE   174 AA;  19832 MW;  1266E35B685B4025 CRC64;
     MYAEYVNQLK NFRIRETQGY NSWCAGYTMS ALLNATYNTN RYNAESVMRY LHPNLRGHDF
     QFTGLTSNEM LRFGRSQGRN TQYLNRMTSY NEVDQLTTNN QGIAVLGKRV ESSDGIHAGH
     AMAVAGNAKV NNGQKVILIW NPWDNGLMTQ DAHSNIIPVS NGDHYEWYAS IYGY