ID   EPIP_STAEP              Reviewed;         461 AA.
AC   P30199;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Epidermin leader peptide-processing serine protease EpiP;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=epiP;
OS   Staphylococcus epidermidis.
OG   Plasmid pTu 32.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TU 3298 / DSM 3095;
RX   PubMed=1740156; DOI=10.1111/j.1432-1033.1992.tb16605.x;
RA   Schnell N., Engelke G., Augustin J., Rosenstein R., Ungermann V., Goetz F.,
RA   Entian K.-D.;
RT   "Analysis of genes involved in the biosynthesis of lantibiotic epidermin.";
RL   Eur. J. Biochem. 204:57-68(1992).
CC   -!- FUNCTION: Protease which cleaves the matured lantibiotic from the
CC       modified prepeptide. {ECO:0000305}.
CC   -!- PATHWAY: Antibiotic biosynthesis; epidermin biosynthesis.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; X62386; CAA44257.1; -; Genomic_DNA.
DR   PIR; S23420; S23420.
DR   AlphaFoldDB; P30199; -.
DR   SMR; P30199; -.
DR   MEROPS; S08.060; -.
DR   UniPathway; UPA00773; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07482; Peptidases_S8_Lantibiotic_specific_protease; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR008357; Lanit_process.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PIRSF; PIRSF037875; Peptidase_S8_lp; 1.
DR   PRINTS; PR01779; LANTIPROCESS.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Plasmid; Protease; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027016"
FT   CHAIN           ?..461
FT                   /note="Epidermin leader peptide-processing serine protease
FT                   EpiP"
FT                   /id="PRO_0000027017"
FT   DOMAIN          121..459
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        149
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        194
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        402
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   461 AA;  51814 MW;  F2770F4F8436D906 CRC64;
     MNKFKFFIVF LILSLVFLQN EYAFGSSLNE ELSYYSVEYD NAKTFKESIK QKNIELTYKI
     PELHTAQIKT SKSKLNSLIK SNKNVKFVNP TCSTCVVEKS VKTGKNLNNK KNGSHDLFDR
     QWDMRKITNE GKSYKLSPDR KKAKVALVDS GVNSSHTDLK SINKIVNEVP KNGFRGSEND
     ESGNKNFEED KLNHGTLVAG QIGANGNLKG VNPGVEMNVY RVFGSKKSEM LWVSKGIIDA
     ANDDNDVINV SLGNYLIKDN QNKKKLRDDE KVDYDALQKA INYAQKKGSI VVAAVGNDGI
     NVKKVKEINK KRNLNSKTSK KVYDSPANLN NVMTVGSIDD NDYISEFSNY GNNFIDLMTI
     GGSYKLLDKY GKDAWLEKGY MQKQSVLSTS SNGRYIYQSG TSLAAPKVSG ALALEIDKYQ
     LKDQPETAIE LFKKKGIEKE KYMDKKHYGN GKLDVYKLLK E