ID   PPCE_AERHY              Reviewed;         690 AA.
AC   Q06903;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Prolyl endopeptidase;
DE            Short=PE;
DE            EC=3.4.21.26;
DE   AltName: Full=Post-proline cleaving enzyme;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=AK-9;
RX   PubMed=8370677; DOI=10.1093/oxfordjournals.jbchem.a124120;
RA   Kanatani A., Yoshimoto T., Kitazono A., Kokubo T., Tsuru D.;
RT   "Prolyl endopeptidase from Aeromonas hydrophila: cloning, sequencing, and
RT   expression of the enzyme gene, and characterization of the expressed
RT   enzyme.";
RL   J. Biochem. 113:790-796(1993).
CC   -!- FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl
CC       residues within peptides that are up to approximately 30 amino acids
CC       long. Has an absolute requirement for an X-Pro bond in the trans
CC       configuration immediately preceding the Pro-Y scissible bond.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC         EC=3.4.21.26;
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR   EMBL; D14005; BAA03105.1; -; Genomic_DNA.
DR   PIR; JN0585; JN0585.
DR   AlphaFoldDB; Q06903; -.
DR   SMR; Q06903; -.
DR   STRING; 1448139.AI20_15415; -.
DR   ESTHER; aerhy-ppce; S9N_PPCE_Peptidase_S9.
DR   PRIDE; Q06903; -.
DR   eggNOG; COG1505; Bacteria.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Serine protease.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..690
FT                   /note="Prolyl endopeptidase"
FT                   /id="PRO_0000122399"
FT   ACT_SITE        538
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        657
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
SQ   SEQUENCE   690 AA;  76515 MW;  854677C4AE753EB6 CRC64;
     MSGKARLHYP VTRQSEQLDH YFGQAVADPY RWLEDDRSPE TEAWVKAQNR VTQDYLAQIP
     FRDAIKGKLA TSWNYAKEGA PFREGRYHYF FKNDGLQNQN VLCGQLAGKP AEVFLDPNLL
     SPDGTTALDQ LSFSRDGKTL AYSLSLAGSD WREIHLMDVE SKQPLETPLR DVKFSGISWL
     GNEGFFYSSY DKPDGSELSA RTDQHKLYFH RLGTAQEEDR LVFGAIPAQR HRYVGATVTE
     DDRYLLISAA DSTSGNRLYV KDLTREGAPL LTVQGDLAAD VSLVDNKGSR LYLLTNRDAP
     NRRLVTVEAD NPGPEQWRDL IPERQQVLTV HSGGGYLFAE YMVDATARVE QFDHDGKRVR
     EVGLPGLGSV SGFNGKQDDP ALYFGFENYA QPPTLYKFEP NSGAISLYRA SAAPFKPEDY
     VSEQRFYRSK DGTRVPLIIS YRKGLKLDGS NPTILYGYGG FDVSLTPSFS VSVANWLDLG
     GVYAVANLRG GGEYGQAWHL AGTRMNKQNV FDDFIAAAEY LKAEGYTRTD RLAIRGGSNG
     GLLVGAVMTQ RPDLMRVACQ AVGVLDMLRY HTFTAGAGWA YDYGTSADSE AMFDYLKGYS
     PLHSVRAGVS YPSTLVTTAD HDDRVVPAHS FKFAATLQAD DAGPHPQLIR IETNAGHGAG
     TPVAKLIEQS ADIYAFTLFE MGYRQLPRQP