ID   PIP_LACH4               Reviewed;         294 AA.
AC   A8YWL3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Proline iminopeptidase {ECO:0000312|EMBL:ABX26375.1};
DE            Short=PIP {ECO:0000250|UniProtKB:P52278};
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000250|UniProtKB:P52278};
DE            Short=PAP {ECO:0000250|UniProtKB:P52278};
GN   Name=pip {ECO:0000250|UniProtKB:P52278}; OrderedLocusNames=lhv_0102;
OS   Lactobacillus helveticus (strain DPC 4571).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=405566;
RN   [1] {ECO:0000312|EMBL:ABX26375.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 4571;
RX   PubMed=17993529; DOI=10.1128/jb.01295-07;
RA   Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA   McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA   Beresford T., Ross R.P.;
RT   "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT   selective gene loss and IS element expansion.";
RL   J. Bacteriol. 190:727-735(2008).
CC   -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC       {ECO:0000250}.
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}.
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DR   EMBL; CP000517; ABX26375.1; -; Genomic_DNA.
DR   RefSeq; WP_012211252.1; NC_010080.1.
DR   AlphaFoldDB; A8YWL3; -.
DR   SMR; A8YWL3; -.
DR   STRING; 405566.lhv_0102; -.
DR   ESTHER; lache-pip; Proline_iminopeptidase.
DR   MEROPS; S33.021; -.
DR   EnsemblBacteria; ABX26375; ABX26375; lhv_0102.
DR   KEGG; lhe:lhv_0102; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_15_1_9; -.
DR   OMA; TWYRVTG; -.
DR   Proteomes; UP000000790; 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.
FT   CHAIN           1..294
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000406325"
FT   DOMAIN          27..277
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        105
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   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