ID   PIP_LACRL               Reviewed;         291 AA.
AC   C7TMK0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Proline iminopeptidase {ECO:0000312|EMBL:CAR91434.1};
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=pepIP {ECO:0000312|EMBL:CAR91434.1};
GN   OrderedLocusNames=LC705_02595;
OS   Lacticaseibacillus rhamnosus (strain Lc 705) (Lactobacillus rhamnosus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=568704;
RN   [1] {ECO:0000312|EMBL:CAR91434.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lc 705;
RX   PubMed=19805152; DOI=10.1073/pnas.0908876106;
RA   Kankainen M., Paulin L., Tynkkynen S., von Ossowski I., Reunanen J.,
RA   Partanen P., Satokari R., Vesterlund S., Hendrickx A.P., Lebeer S.,
RA   De Keersmaecker S.C., Vanderleyden J., Hamalainen T., Laukkanen S.,
RA   Salovuori N., Ritari J., Alatalo E., Korpela R., Mattila-Sandholm T.,
RA   Lassig A., Hatakka K., Kinnunen K.T., Karjalainen H., Saxelin M.,
RA   Laakso K., Surakka A., Palva A., Salusjarvi T., Auvinen P., de Vos W.M.;
RT   "Comparative genomic analysis of Lactobacillus rhamnosus GG reveals pili
RT   containing a human- mucus binding protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17193-17198(2009).
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; FM179323; CAR91434.1; -; Genomic_DNA.
DR   RefSeq; WP_014571653.1; NC_013199.1.
DR   AlphaFoldDB; C7TMK0; -.
DR   SMR; C7TMK0; -.
DR   ESTHER; lacrl-pip; Proline_iminopeptidase.
DR   KEGG; lrl:LC705_02595; -.
DR   HOGENOM; CLU_020336_15_1_9; -.
DR   OMA; TWYRVTG; -.
DR   BRENDA; 3.4.11.5; 2891.
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..291
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000406327"
FT   DOMAIN          30..274
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        103
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P96084"
FT   ACT_SITE        242
FT                   /evidence="ECO:0000250|UniProtKB:O32449"
FT   ACT_SITE        269
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P96084"
SQ   SEQUENCE   291 AA;  33109 MW;  5622EC0CE9816CC8 CRC64;
     MKIKEGYMPF HEYKTYYRIV GEPSADKAPL LIHGGPGSSH NYFELMDDYA ETGRQLIMYD
     QVGCGKSSLP EDPGVYVKET WAEELVALRK FLHLDELHML GQSWGGMLEM YYLTSFDPQG
     IKSVMIDGSP ASIKLWVQEQ HRLIKYLSYE DRAAIAEAER TGDFTNVKYL AANDRYMEKY
     CWDDPDENSP EPLRRPTNGK RASLIAEGPN EFTENGTISD FDVTDQLHKI HVPVLVTSGT
     DDLCTPLIAK SVVDHIPGAK WHLFANSRHL ALLDQHDEFI HVLDQWLAAN D