ID   PIP_LACAC               Reviewed;         293 AA.
AC   Q5FMT1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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 {ECO:0000312|EMBL:AAV41993.1};
DE            Short=PAP {ECO:0000250|UniProtKB:P52278};
GN   Name=pip {ECO:0000250|UniProtKB:P52278};
GN   Synonyms=pepI {ECO:0000250|UniProtKB:P52278}; OrderedLocusNames=LBA0092;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1] {ECO:0000312|EMBL:AAV41993.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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}.
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DR   EMBL; CP000033; AAV41993.1; -; Genomic_DNA.
DR   RefSeq; WP_003548604.1; NC_006814.3.
DR   RefSeq; YP_193024.1; NC_006814.3.
DR   AlphaFoldDB; Q5FMT1; -.
DR   SMR; Q5FMT1; -.
DR   STRING; 272621.LBA0092; -.
DR   ESTHER; lacac-pip; Proline_iminopeptidase.
DR   MEROPS; S33.021; -.
DR   EnsemblBacteria; AAV41993; AAV41993; LBA0092.
DR   GeneID; 56941707; -.
DR   KEGG; lac:LBA0092; -.
DR   PATRIC; fig|272621.13.peg.88; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_15_1_9; -.
DR   OMA; TWYRVTG; -.
DR   BioCyc; LACI272621:G1G49-92-MON; -.
DR   BRENDA; 3.4.11.5; 2846.
DR   Proteomes; UP000006381; 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..293
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000406321"
FT   DOMAIN          28..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   293 AA;  33830 MW;  6E7D3D3D1D782006 CRC64;
     MEIIEGKMPF MGYETHYRIV GRRSEKSPLV LLHGGPGSTH NYFEVLDKLA KIDDRRIIMY
     DQLGCGNSSI PDDHPELYTK ETWVKELKTL REHLALRKIH LLGQSWGGML AIIYMCDYHP
     EGIQSLILSS TLSSASLWSK ELHRMIKYLP IEEQAAIHRA ELTDTFTEPD YLKANEHFMN
     QHAIDMKKKW PECVMREKKG GTVAYETAWG PNEYTPEGNL HDYEYTDQLS KIKVPTLITS
     GTDDLCTPYV AKTMHDHIAG SQWKLFENCS HMSFVQKTDE YIAMLKKWLD AND