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   20-JAN-2009, entry version 46.
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   MEDLINE=93380910; PubMed=8370677;
RA   Kanatani A., Yoshimoto T., Kitazono A., Kokubo T., Tsuru D.;
RT   "Prolyl endopeptidase from Aeromonas hydrophila: cloning, sequencing,
RT   and expression of the enzyme gene, and characterization of the
RT   expressed 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
CC       acids long. Has an absolute requirement for an X-Pro bond in the
CC       trans configuration immediately preceding the Pro-Y scissible
CC       bond.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in
CC       oligopeptides.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family.
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DR   EMBL; D14005; BAA03105.1; -; Genomic_DNA.
DR   PIR; JN0585; JN0585.
DR   HSSP; P23687; 1O6G.
DR   MEROPS; S09.001; -.
DR   BRENDA; 3.4.21.26; 3060.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   InterPro; IPR004106; Peptidase_S9A_N.
DR   PANTHER; PTHR11757; Peptidase_S9A; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
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      1       Removed.
FT   CHAIN         2    690       Prolyl endopeptidase.
FT                                /FTId=PRO_0000122399.
FT   ACT_SITE    538    538       Charge relay system (By similarity).
FT   ACT_SITE    657    657       Charge relay system (By similarity).
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
//