ID   PIP_LACCS               Reviewed;         293 AA.
AC   D5H0J3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Proline iminopeptidase {ECO:0000312|EMBL:CBL49528.1};
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};
GN   Synonyms=pepI {ECO:0000312|EMBL:CBL49528.1}; OrderedLocusNames=LCRIS_00081;
OS   Lactobacillus crispatus (strain ST1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=748671;
RN   [1] {ECO:0000312|EMBL:CBL49528.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST1;
RX   PubMed=20435723; DOI=10.1128/jb.00399-10;
RA   Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P.,
RA   Edelman S., Westerlund-Wikstrom B., Korhonen T.K., Paulin L., Kankainen M.;
RT   "Genome sequence of Lactobacillus crispatus ST1.";
RL   J. Bacteriol. 192:3547-3548(2010).
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; FN692037; CBL49528.1; -; Genomic_DNA.
DR   RefSeq; WP_013085645.1; NC_014106.1.
DR   AlphaFoldDB; D5H0J3; -.
DR   SMR; D5H0J3; -.
DR   STRING; 748671.LCRIS_00081; -.
DR   ESTHER; laccs-pip; Proline_iminopeptidase.
DR   EnsemblBacteria; CBL49528; CBL49528; LCRIS_00081.
DR   KEGG; lcr:LCRIS_00081; -.
DR   PATRIC; fig|748671.3.peg.74; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_15_1_9; -.
DR   OMA; TWYRVTG; -.
DR   OrthoDB; 1282004at2; -.
DR   Proteomes; UP000002371; 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..293
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000406323"
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;  33827 MW;  274613BC86A4B893 CRC64;
     MEVIEGKMPF MGYETYYRIV GRRSEKTPLV LLHGGPGSSH NYFEVLDKLA EIDNRRIIMY
     DQLGCGKSSI PDDHPELYTK ETWVKELMAL REHLALRKIH LLGQSWGGML ALIYMCDYHP
     VGIQSLILSS TLSSASLWSK ELHRMIKYLP IEEQAAIHRA ELTSNFNDPD YLKANEHFMN
     QHAIDMTKTW PECVMRKKCG GIVAYETAWG PNEYTPEGNL HDYEYTEKLG KIKIPTLITS
     GTDDLCTPYV AKTMQDHLAG SKWQLFENCG HMSFVEKTDE YVEMLRKWLD QHD