ID   PIP_CHIPD               Reviewed;         299 AA.
AC   C7PDD8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Proline iminopeptidase {ECO:0000250|UniProtKB:O05420};
DE            Short=PIP {ECO:0000250|UniProtKB:O05420};
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000250|UniProtKB:O05420};
DE            Short=PAP {ECO:0000250|UniProtKB:O05420};
GN   OrderedLocusNames=Cpin_0261;
OS   Chitinophaga pinensis (strain ATCC 43595 / DSM 2588 / LMG 13176 / NBRC
OS   15968 / NCIMB 11800 / UQM 2034).
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=485918;
RN   [1] {ECO:0000312|EMBL:ACU57761.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43595 / DSM 2588 / LMG 13176 / NBRC 15968 / NCIMB 11800 / UQM
RC   2034;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Sims D., Meinche L., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Chitinophaga pinensis DSM 2588.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC       {ECO:0000250|UniProtKB:O05420}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000250|UniProtKB:O05420};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O05420}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACU57761.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001699; ACU57761.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C7PDD8; -.
DR   SMR; C7PDD8; -.
DR   STRING; 485918.Cpin_0261; -.
DR   ESTHER; chipd-pip; Proline_iminopeptidase.
DR   EnsemblBacteria; ACU57761; ACU57761; Cpin_0261.
DR   KEGG; cpi:Cpin_0261; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_15_0_10; -.
DR   Proteomes; UP000002215; 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.
FT   CHAIN           1..299
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_5000508838"
FT   DOMAIN          26..272
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        103
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P96084"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000250|UniProtKB:O32449"
FT   ACT_SITE        272
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P96084"
SQ   SEQUENCE   299 AA;  33848 MW;  45B4FFF392FC70F9 CRC64;
     MIPIKTPKGV FNVWTKRIGN NPKVKVLLLA GGPGFPHDYL EAFESYFPGE GIEFYYYDEL
     GNGNSDKPGD SSRYNVASAV DEVEQVRQAL KLDSSNFYLF GHSWGGALGM EYAIKYQNNL
     KALIVSNMVA SGKEFNRYVQ QVLVKQLPPA ILDTINDLSA RNDYSNPKYS ELVTRHFYAR
     FICRLPLDQW PEPLNRAFSK VNTPYYLTLQ GPSELGIIGS LQTWDISARL KEIAVPALFI
     GAGYDEMDPE HIKWMSQQVP HGQFLYCANG SHLSMYDQQP FYMNGIIRFI KEVNNSSAN