ID   PIP_LACPL               Reviewed;         287 AA.
AC   Q890D8; F9USR8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Proline iminopeptidase {ECO:0000250|UniProtKB:P52278};
DE            Short=PIP {ECO:0000250|UniProtKB:P52278};
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase;
DE            Short=PAP {ECO:0000250|UniProtKB:P52278};
GN   Name=pip {ECO:0000250|UniProtKB:P52278}; Synonyms=pepI;
GN   OrderedLocusNames=lp_0088;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
CC   -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC       {ECO:0000250|UniProtKB:P52278}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000250|UniProtKB:P52278};
CC   -!- SUBCELLULAR LOCATION: Cell envelope {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL935263; CCC77649.1; -; Genomic_DNA.
DR   RefSeq; YP_004888163.1; NC_004567.2.
DR   AlphaFoldDB; Q890D8; -.
DR   SMR; Q890D8; -.
DR   STRING; 220668.lp_0088; -.
DR   ESTHER; lacpl-PEPI; Proline_iminopeptidase.
DR   MEROPS; S33.021; -.
DR   EnsemblBacteria; CCC77649; CCC77649; lp_0088.
DR   KEGG; lpl:lp_0088; -.
DR   PATRIC; fig|220668.9.peg.72; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_15_1_9; -.
DR   PhylomeDB; Q890D8; -.
DR   BioCyc; LPLA220668:G1GW0-71-MON; -.
DR   BRENDA; 3.4.11.5; 2849.
DR   Proteomes; UP000000432; Chromosome.
DR   GO; GO:0031975; C:envelope; IEA:UniProtKB-SubCell.
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..287
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000406326"
FT   DOMAIN          22..271
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        98
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        238
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   287 AA;  32411 MW;  7A809B182D7D1D3B CRC64;
     MPFNGYQTYY RIVGDRQSNK TPLVLLHGGP GSTHNYFEGF DDLAAQTGRP IVMYDQLGCG
     RSSIPDDDQL WQAAMWVAEL RALRTYLDLP EIHLLGQSWG GMLAIIYGCD YRPQGIKSLI
     LASTLSSARL WAQEQHRMIR LMSPVDQSAI ATAERLQDFT GAAYLTANQH FMTQHASGPI
     TADDPEFLRR SKRVGTTAYN VAWGPNEYNP TGTLADYEYT DRLQYLQMPT LVTSGTDDLC
     TPLVAKTMVD QLPHATWTLF PRSRHMAFID ENTAYMTRLR HWLAAHD