ID   PIP_LACHE               Reviewed;         294 AA.
AC   P52278;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
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 helveticus (Lactobacillus suntoryeus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=53/7;
RX   PubMed=9004508; DOI=10.1099/13500872-142-12-3459;
RA   Varmanen P., Rantanen T., Palva A.;
RT   "An operon from Lactobacillus helveticus composed of a proline
RT   iminopeptidase gene (pepI) and two genes coding for putative members of the
RT   ABC transporter family of proteins.";
RL   Microbiology 142:3459-3468(1996).
CC   -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC       Hydrolyzes only di- and tripeptides with proline in the first position.
CC       {ECO:0000269|PubMed:9004508}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000269|PubMed:9004508};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.8 mM for Pro-pNA (at 40 degrees Celsius and pH 7.5)
CC         {ECO:0000269|PubMed:9004508};
CC         Vmax=350 mmol/min/mg enzyme with Pro-pNA as substrate
CC         {ECO:0000269|PubMed:9004508};
CC       pH dependence:
CC         Optimum pH is 7.5. At pH values above 7.5, the activity sharply
CC         decreases. {ECO:0000269|PubMed:9004508};
CC       Temperature dependence:
CC         Optimum activity at 40 degrees Celsius. {ECO:0000269|PubMed:9004508};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9004508}.
CC   -!- SUBCELLULAR LOCATION: Cell envelope {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; Z56283; CAA91231.1; -; Genomic_DNA.
DR   RefSeq; WP_012211252.1; NZ_WCGH01000028.1.
DR   AlphaFoldDB; P52278; -.
DR   SMR; P52278; -.
DR   STRING; 326425.lhe_0115; -.
DR   ESTHER; lache-pip; Proline_iminopeptidase.
DR   MEROPS; S33.021; -.
DR   eggNOG; COG2267; Bacteria.
DR   OMA; TWYRVTG; -.
DR   BRENDA; 3.4.11.5; 2870.
DR   SABIO-RK; P52278; -.
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_0000080838"
FT   DOMAIN          27..277
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        105
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        271
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  33845 MW;  535042DAFD636979 CRC64;
     MEIIEGKMPF MGYETYYRIV GERSEKPPLV LLHGGPGSSH NYFEVLDELA QKDGRRIIMY
     DQLGCGESSI PDDHPELYTK ETWVKELEAL REHLALRKMH LLGQSWGGML AIIYMCDYHP
     EGIQSLILSS TLSSASLWSK ELHRMIKYLP IEEQAAIHRA ELTGNFNDPD YLKANEHFMN
     QHAIDMTKTW PECVMRKKRG GTVAYETAWG PNEYTPEGNL HDYEYTDKLS KIKVPTLITS
     GTDDLCTPYV AKTMQDQIAS SKWRLFEGCG HMSFVEKTDE YVALLQEWLD QHDE