ID   PIP_CLOBH               Reviewed;         293 AA.
AC   A5I3F5; A7G4W3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Proline iminopeptidase {ECO:0000312|EMBL:CAL83573.1};
DE            Short=PIP {ECO:0000250|UniProtKB:P46542};
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000312|EMBL:ABS36268.1};
DE            Short=PAP {ECO:0000250|UniProtKB:P46542};
GN   Name=pip {ECO:0000250|UniProtKB:P46542};
GN   Synonyms=pepIP {ECO:0000312|EMBL:CAL83573.1};
GN   OrderedLocusNames=CBO2031, CLC_1977;
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771;
RN   [1] {ECO:0000312|EMBL:CAL83573.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
RN   [2] {ECO:0000312|EMBL:ABS36268.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; AM412317; CAL83573.1; -; Genomic_DNA.
DR   EMBL; CP000727; ABS36268.1; -; Genomic_DNA.
DR   RefSeq; WP_011986559.1; NC_009698.1.
DR   RefSeq; YP_001254533.1; NC_009495.1.
DR   RefSeq; YP_001387828.1; NC_009698.1.
DR   AlphaFoldDB; A5I3F5; -.
DR   SMR; A5I3F5; -.
DR   ESTHER; clobh-pip; Proline_iminopeptidase.
DR   MEROPS; S33.021; -.
DR   GeneID; 5186286; -.
DR   KEGG; cbh:CLC_1977; -.
DR   KEGG; cbo:CBO2031; -.
DR   PATRIC; fig|413999.7.peg.2003; -.
DR   HOGENOM; CLU_020336_15_1_9; -.
DR   OMA; TWYRVTG; -.
DR   PRO; PR:A5I3F5; -.
DR   Proteomes; UP000001986; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
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_0000406317"
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;  33401 MW;  10C1887EAC68FDF4 CRC64;
     MKITEGYMPY LEYKTYYRIV GECTGNKKPL VLLHGGPGST HNYFEVLDKV AEDGRAVIMY
     DQLGCGLSAT PSRPDLWNAK TWIEELIQLR KHLGLDEIHL LGQSWGGMQA IQYACEYKPE
     GIKSYILSST LPAASLWEKE QRRRVAYLPQ EMQDAIAKAE KAGDYSSKEY QEAEAEFMLR
     HCAGAVGPDS PECLRRPKVA GTEAYVTAWG QNEFSPSGTL KNFDFMKEIE DIKEPCLITS
     GLLDLCSPLV AKTMYDKIPN SEWELFEFSR HMPFVEENEK YIEVLNKWLN KND