ID   POPB_AMABI              Reviewed;         730 AA.
AC   E2JFG2;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Dual function macrocyclase-peptidase POPB {ECO:0000250|UniProtKB:H2E7Q8};
DE            EC=3.4.21.26 {ECO:0000250|UniProtKB:H2E7Q8};
DE   AltName: Full=Prolyl oligopeptidase B {ECO:0000303|PubMed:20889720};
DE            Short=POP B {ECO:0000303|PubMed:20889720};
DE   AltName: Full=Toxin-processing prolyl oligopeptidase {ECO:0000303|PubMed:20889720};
GN   Name=POPB {ECO:0000303|PubMed:20889720};
OS   Amanita bisporigera (Destroying angel).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX   NCBI_TaxID=87325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=20889720; DOI=10.1128/ec.00161-10;
RA   Luo H., Hallen-Adams H.E., Scott-Craig J.S., Walton J.D.;
RT   "Colocalization of amanitin and a candidate toxin-processing prolyl
RT   oligopeptidase in Amanita basidiocarps.";
RL   Eukaryot. Cell 9:1891-1900(2010).
CC   -!- FUNCTION: Dual function macrocyclase-peptidase involved in the
CC       biosynthesis of the highly toxic amanitin toxin family of macrocycles
CC       (PubMed:20889720). Cleaves peptide bonds on the C-terminal side of
CC       prolyl residues (By similarity). The enzyme first removes 10 residues
CC       from the N-terminus of a 35-residue substrate (By similarity).
CC       Conformational trapping of the 25 amino-acid peptide forces the enzyme
CC       to release this intermediate rather than proceed to macrocyclization
CC       (By similarity). The enzyme rebinds the 25 amino-acid peptide in a
CC       different conformation and catalyzes macrocyclization of the N-terminal
CC       eight residues (By similarity). {ECO:0000250|UniProtKB:H2E7Q8,
CC       ECO:0000305|PubMed:20889720}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC         EC=3.4.21.26;
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48147}.
CC   -!- TISSUE SPECIFICITY: Expressed in the pileus (cap) and lamellae where it
CC       colocalizes with amanitin (PubMed:20889720).
CC       {ECO:0000269|PubMed:20889720}.
CC   -!- SIMILARITY: Belongs to the peptidase S9A 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; HQ225841; ADN19205.1; -; mRNA.
DR   AlphaFoldDB; E2JFG2; -.
DR   SMR; E2JFG2; -.
DR   MEROPS; S09.077; -.
DR   BRENDA; 3.4.21.26; 12947.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protease; Serine protease.
FT   CHAIN           1..730
FT                   /note="Dual function macrocyclase-peptidase POPB"
FT                   /id="PRO_0000443716"
FT   ACT_SITE        577
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        661
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        698
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
SQ   SEQUENCE   730 AA;  81671 MW;  9C94AEFD8262FEAF CRC64;
     MPPTPWAPHS YPPTRRSDHV DVYQSASRGE VPVPDPYQWL EENSNEVDEW TTAQTAFTQG
     YLDKNADRQK LEEKFRASKD YVKFSAPTLL DSGHWYWFYN SGVQSQAVLY RSKKPVLPDF
     QRGTRKVGEV YFDPNVLSAD GTAIMGTCRF SPSGEYFAYA VSHLGVDYFT IYVRPTSSSL
     SQAPEAEGGD GRLSDGVKWC KFTTITWTKD SKGFLYQRYP ARESLVAKDR DKDAMVCYHR
     VGTTQLEDII VQQDKENPDW TYGTDASEDG KYIYLVVYKD ASKQNLLWVA EFDKDGVKPE
     IPWRKVINEF GADYHVITNH GSLIYVKTNV NAPQYKVVTI DLSTGEPEIR DFIPEQKDAK
     LTQVKCVNKG YFVAIYKRNV KDEIYLYSKA GDQLSRLASD FIGVASITNR EKQPHSFLTF
     SGFNTPGTIS RYDFTAPDTQ RLSILRTTKL NGLNADDFES TQVWYKSKDG TKVPMFIVRH
     KSTKFDGTAP AIQNGYGGFA ITADPFFSPI MLTFMQTYGA ILAVPNIRGG GEFGGEWHKA
     GRRETKGNTF DDFIAAAQFL VKNKYAAPGK VAITGASNGG FLVCGSVVRA PEGTFGAAVS
     EGGVADLLKF NKFTGGMAWT SEYGNPFIKE DFDFVQALSP VHNVPKDRVL PATLLMTNAG
     DDRVVPMHSL KFVANLQYNV PQNPHPLLIR VDKSWLGHGF GKTTDKHTKD AADKWSFVAQ
     SLGLEWKTVD