ID   PPCF_ELIMR              Reviewed;         705 AA.
AC   P27195;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Prolyl endopeptidase;
DE            EC=3.4.21.26;
DE   AltName: Full=Post-proline cleaving enzyme;
DE   AltName: Full=Proline-specific endopeptidase;
DE            Short=PE;
DE            Short=PSE;
DE   Flags: Precursor;
OS   Elizabethkingia miricola (Chryseobacterium miricola).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Elizabethkingia.
OX   NCBI_TaxID=172045;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 33958;
RX   PubMed=1569074; DOI=10.1016/s0021-9258(18)42426-x;
RA   Chevallier S., Goeltz P., Thibault P., Banville D., Gagnon J.;
RT   "Characterization of a prolyl endopeptidase from Flavobacterium
RT   meningosepticum. Complete sequence and localization of the active-site
RT   serine.";
RL   J. Biol. Chem. 267:8192-8199(1992).
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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR   EMBL; M81461; AAA24925.1; -; Genomic_DNA.
DR   AlphaFoldDB; P27195; -.
DR   SMR; P27195; -.
DR   STRING; 172045.KS04_15965; -.
DR   ESTHER; elimr-ppcf; S9N_PPCE_Peptidase_S9.
DR   eggNOG; COG1505; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; Periplasm; Protease; Serine protease;
KW   Signal.
FT   SIGNAL          1..20
FT   CHAIN           21..705
FT                   /note="Prolyl endopeptidase"
FT                   /id="PRO_0000027208"
FT   ACT_SITE        556
FT                   /note="Charge relay system"
FT   ACT_SITE        675
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
SQ   SEQUENCE   705 AA;  78790 MW;  36925D9A8783E03A CRC64;
     MKYKKLSVAV AAFAFAAVSA QNSNSLKYPE TKKVNHTDTY FGNQVSDPYR WLEDDRAEDT
     KAWVQQEVKF TQDYLAQIPF RGQIKKQLLD IWNYEKISAP FKKGKYTYFY KNDGLQAQSV
     LYRKDASGKT EVFLDPNKFS DKGTTSLANL SFNKKGTLVA YSISEGGSDW NKIIILDAET
     KKQIDETLLD VKFSGISWLG DEGFFYSSYD KPKDGSVLSG MTDKHKVYFH KLGTKQSQDE
     LIIGGDKFPR RYLSGYVTED QRYLVVSAAN ATNGNELYIK DLKNKTDFIP IITGFESNVG
     LVDTDGDTLF LHTDKNAPNM RMVKTTIQNP KPETWKDVIA ETSEPMRVNS GGGYFFATYM
     KDALSQIKQY DKTGKLVREI KLPGSGTAGG FGGEKTEKEL YYSFTNYITP PTIFKFSIDS
     GKSEVYQKPK VKFNPENYVS EQVFYTSADG TKIPMMISNK KGLKKDGKNP TILYSYGGFN
     ISLQPAFSVV NAIWMENGGI YAVPNIRGGG EYGKKWHDAG TKQQKKNVFN DFIAAGEYLQ
     KNGYTSKDYM ALSGRSNGGL LVGATMTMRP DLAKVAFPGV GVLDMLRYNK FTAGAGWAYD
     YGTAEDSKEM FEYLKSYSPV HNVKAGTCYP STMVITSDHD DRVVPAHSFK FGAELQAKQA
     CKNPVLIRIE TNAGHGAGRS TEQVVMENAD LLSFALYEMG IKNLK