ID   PIP_CLOD6               Reviewed;         293 AA.
AC   Q184M8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Proline iminopeptidase {ECO:0000312|EMBL:CAJ69934.1};
DE            Short=PIP {ECO:0000250|UniProtKB:P46542};
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000250|UniProtKB:P46542};
DE            Short=PAP {ECO:0000250|UniProtKB:P46542};
GN   Name=pip {ECO:0000250|UniProtKB:P46542};
GN   Synonyms=pepI {ECO:0000312|EMBL:CAJ69934.1}; OrderedLocusNames=CD630_30410;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1] {ECO:0000312|EMBL:CAJ69934.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
CC   -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC       {ECO:0000250|UniProtKB:P46542}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000250|UniProtKB:P46542};
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000255}.
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DR   EMBL; AM180355; CAJ69934.1; -; Genomic_DNA.
DR   RefSeq; WP_003439900.1; NZ_CP010905.2.
DR   RefSeq; YP_001089556.1; NC_009089.1.
DR   AlphaFoldDB; Q184M8; -.
DR   SMR; Q184M8; -.
DR   STRING; 272563.CD630_30410; -.
DR   ESTHER; pepd6-pip; Proline_iminopeptidase.
DR   MEROPS; S33.021; -.
DR   EnsemblBacteria; CAJ69934; CAJ69934; CD630_30410.
DR   GeneID; 66355439; -.
DR   KEGG; cdf:CD630_30410; -.
DR   KEGG; pdc:CDIF630_03325; -.
DR   PATRIC; fig|272563.120.peg.3207; -.
DR   eggNOG; COG2267; Bacteria.
DR   OMA; TWYRVTG; -.
DR   PhylomeDB; Q184M8; -.
DR   BioCyc; PDIF272563:G12WB-3203-MON; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002410; Peptidase_S33.
DR   InterPro; IPR005945; Pro_imino_pep.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF005539; Pept_S33_TRI_F1; 1.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01250; pro_imino_pep_2; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..293
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000406318"
FT   DOMAIN          28..277
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P96084"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000250|UniProtKB:O32449"
FT   ACT_SITE        271
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P96084"
SQ   SEQUENCE   293 AA;  33663 MW;  5B2A1900C5A9F2F4 CRC64;
     MKITEGYMPF KGFKTYYRIV GENTEGKKPL VLLHGGPGST HNYFEVLDKI AESGRQVIMY
     DQIGCGNSFV EGHPELFNAD TWIEELIELR KHLGLDEIHL LGQSWGGMQA IWYAIEYKPK
     GIKSYILSST LSSAKLWEKE QKRRISYMSE VDQKALLDAV NTGDYSSKEY NDALERFMEM
     YCAGEVTEDS PECLRRPKKS GSEAYIVGWG QNEFSPTGTL SGYEFTDRLH EIKEPCLVTS
     GAIDLCSPYI AKTMYDRIPN SKWELFEYSR HMPFVEENEK YIKVLTEWLN AND