ID   PIP_LACDL               Reviewed;         294 AA.
AC   P46542;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Proline iminopeptidase;
DE            Short=PIP;
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase;
DE            Short=PAP;
GN   Name=pip; Synonyms=pepI;
OS   Lactobacillus delbrueckii subsp. lactis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=29397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   ACTIVITY REGULATION.
RC   STRAIN=DSM 7290;
RX   PubMed=8025678; DOI=10.1099/13500872-140-5-1133;
RA   Klein J.R., Schmidt U., Plapp R.;
RT   "Cloning, heterologous expression, and sequencing of a novel proline
RT   iminopeptidase gene, pepI, from Lactobacillus delbrueckii subsp. lactis DSM
RT   7290.";
RL   Microbiology 140:1133-1139(1994).
CC   -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC       Cleaves Pro-betaNA (L-prolyl-beta-naphthylamide) effectively.
CC       {ECO:0000269|PubMed:8025678}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000269|PubMed:8025678};
CC   -!- ACTIVITY REGULATION: Inhibited by 3,4-DCI, but no significant effect on
CC       enzyme activity by pepstatin A, E-64, 1,10-phenanthroline or EDTA.
CC       {ECO:0000269|PubMed:8025678}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell envelope {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; Z26948; CAA81556.1; -; Genomic_DNA.
DR   PIR; A59087; A59087.
DR   AlphaFoldDB; P46542; -.
DR   SMR; P46542; -.
DR   ESTHER; lacdl-pip; Proline_iminopeptidase.
DR   MEROPS; S33.021; -.
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   1: Evidence at protein level;
KW   Aminopeptidase; Hydrolase; Protease.
FT   CHAIN           1..294
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000080837"
FT   DOMAIN          28..278
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        272
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  32879 MW;  A5E369D34F1620F3 CRC64;
     MQITEKYLPF GNWQTYCRIV GEATDRAPLL LLHGGPGSSH NYFEVLDQVA EKSGRQVIMY
     DQLGCGNSSI PDDQAETAYT AQTWVKELEN VREQLGLDQI HLLGQSWGGM LALIYLCDYQ
     PKGVKSLILS STLASAKLWS QELHRLIKYL PKGEQAAIKE AETTGNYDSP AYQAANAHFM
     DQHAINVTPD LPEPVLRKKK GGNLAYLTGW GPNEYTPIGN LHGYEYTDRL KDLDLPALIT
     SGTDDLCTPL VAKSMYDHLP NARWELFAGC GHMPFVQENA KYQELLSDWL ISQD