ID   PPCE_ELIME              Reviewed;         705 AA.
AC   P27028;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 106.
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;
GN   Name=f1pep1;
OS   Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Elizabethkingia.
OX   NCBI_TaxID=238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1840588; DOI=10.1093/oxfordjournals.jbchem.a123682;
RA   Yoshimoto T., Kanatani A., Shimoda T., Inaoka T., Kokubo T., Tsuru D.;
RT   "Prolyl endopeptidase from Flavobacterium meningosepticum: cloning and
RT   sequencing of the enzyme gene.";
RL   J. Biochem. 110:873-878(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7764331; DOI=10.1007/bf00170434;
RA   Diefenthal T., Dargatz H., Witte V., Reipen G., Svendsen I.;
RT   "Cloning of proline-specific endopeptidase gene from Flavobacterium
RT   meningosepticum: expression in Escherichia coli and purification of the
RT   heterologous protein.";
RL   Appl. Microbiol. Biotechnol. 40:90-97(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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR   EMBL; D10980; BAA01755.1; -; Genomic_DNA.
DR   EMBL; X63674; CAA45213.1; -; Genomic_DNA.
DR   PIR; JX0194; JX0194.
DR   RefSeq; WP_016199025.1; NZ_SYWC01000007.1.
DR   AlphaFoldDB; P27028; -.
DR   SMR; P27028; -.
DR   STRING; 1216967.L100_08294; -.
DR   BindingDB; P27028; -.
DR   ChEMBL; CHEMBL6043; -.
DR   ESTHER; flame-ppce; S9N_PPCE_Peptidase_S9.
DR   GeneID; 64003479; -.
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_0000027207"
FT   ACT_SITE        556
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084,
FT                   ECO:0000269|PubMed:1840588"
FT   ACT_SITE        675
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   CONFLICT        110
FT                   /note="S -> C (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        587
FT                   /note="R -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   705 AA;  78707 MW;  BC0EDCBABB328256 CRC64;
     MKYNKLSVAV AAFAFAAVSA QNSNVLKYPE TKKVSHTDTY FGTQVSDPYR WLEDDRAEDT
     KAWVQQEVKF TQDYLAQIPF RDQLKKQLMD IWNYEKISAP FKKGKYTYFS KNDGLQAQSV
     LYRKDAAGKT EVFLDPNKFS EKGTTSLASV SFNKKGTLVA YSISEGGSDW NKIIILDAET
     KKQLDETLLD VKFSGISWLG DEGFFYSSYD KPKEGSVLSG MTDKHKVYFH KLGTKQSQDE
     LIIGGDKFPR RYIGAYVTDD QRYLVVSAAN ATNGNELYIK DLKNKTDFIP IITGFDSNVN
     VADTDGDTLY LFTDKDAPNK RLVKTTIQNP KAETWKDVIA ETSEPLEINT GGGYFFATYM
     KDAIDQVKQY DKNGKLVRAI KLPGSGNASG FGGEKTEKDL YYSFTNYITP PTIFKYNVTT
     GNSEVYQKPK VKFNPENYVS EQVFYTSSDG TKIPMMISYK KGLKKDGKNP TILYSYGGFN
     ISLQPAFSVV NAIWMENGGI YAVPNIRGGG EYGKKWHDAG TKMQKKNVFN DFIAAGEYLQ
     KNGYTSKEYM ALSGRSNGGL LVGATMTMRP DLAKVAFPGV GVLDMLRYNK FTAGAGWAYD
     YGTAEDSKEM FEYLKSYSPV HNVKAGTCYP STMVITSDHD DRVVPAHSFK FGSELQAKQS
     CKNPILIRIE TNAGHGAGRS TEQVVAENAD LLSFALYEMG IKSLK