ID   ECPA_STAEQ              Reviewed;         395 AA.
AC   Q5HKF6;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Extracellular cysteine protease;
DE            EC=3.4.22.-;
DE   AltName: Full=Staphopain;
DE   Flags: Precursor;
GN   Name=ecpA; Synonyms=ecp; OrderedLocusNames=SERP2390;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Secreted {ECO:0000250}.
CC   -!- PTM: Proteolytically cleaved. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C47 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000029; AAW53223.1; -; Genomic_DNA.
DR   RefSeq; WP_002437704.1; NC_002976.3.
DR   AlphaFoldDB; Q5HKF6; -.
DR   SMR; Q5HKF6; -.
DR   STRING; 176279.SERP2390; -.
DR   MEROPS; C47.003; -.
DR   EnsemblBacteria; AAW53223; AAW53223; SERP2390.
DR   GeneID; 50017588; -.
DR   KEGG; ser:SERP2390; -.
DR   eggNOG; ENOG502ZWEC; Bacteria.
DR   HOGENOM; CLU_069043_0_0_9; -.
DR   OMA; NKLENFR; -.
DR   OrthoDB; 743974at2; -.
DR   Proteomes; UP000000531; Chromosome.
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   Gene3D; 3.10.500.10; -; 1.
DR   InterPro; IPR046350; Cystatin_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR008750; Peptidase_C47.
DR   InterPro; IPR028076; Staphopain_pro.
DR   InterPro; IPR037155; Staphopain_pro_sf.
DR   Pfam; PF05543; Peptidase_C47; 1.
DR   Pfam; PF14731; Staphopain_pro; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54403; SSF54403; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   3: Inferred from homology;
KW   Cell wall; Hydrolase; Protease; Reference proteome; Secreted; Signal;
KW   Thiol protease; Virulence; Zymogen.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   PROPEP          31..221
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026575"
FT   CHAIN           222..395
FT                   /note="Extracellular cysteine protease"
FT                   /id="PRO_0000026576"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        341
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   SITE            221..222
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   395 AA;  44701 MW;  90B8331C47688D32 CRC64;
     MKKKLSYMIT IMLAFTLSLA LGLFFNSAHA DSLPQKNGAN QKTTKVTVSN KDVPDAVRKL
     AEEQYLSRVA LLDKASNHKA TSYTLGEPFK IYKFNKESDG NYYYPVLNKK GDVVYVVTIS
     PNPSNSKASK QQNNYSINVS PFLSKILNQY KNQKITILTN TKGYFALTED GKVTLVLKTP
     RNNEKTYENA TESTKPKDLN DFKQTASVTK PTLEYQSTRN EMYAEYVNQL KNFRIRETQG
     YNSWCAGYTM SALLNATYNT NRYNAESVMR YLHPNLRGHD FQFTGLTSNE MLRFGRSQGR
     NTQYLNRMTS YNEVDQLTTN NQGIAVLGKR VESSDGIHAG HAMAVAGNAK VNNGQKVILI
     WNPWDNGLMT QDAHSNIIPV SNGDHYEWYA SIYGY