ID   PIP_LEVBA               Reviewed;         299 AA.
AC   Q03NE0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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:0000250|UniProtKB:P52278};
DE            Short=PAP {ECO:0000250|UniProtKB:P52278};
GN   Name=pip {ECO:0000250|UniProtKB:P52278};
GN   Synonyms=pepI {ECO:0000250|UniProtKB:P52278}; OrderedLocusNames=LVIS_2232;
OS   Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS   1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=387344;
RN   [1] {ECO:0000312|EMBL:ABJ65282.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB
RC   947 / NCTC 947;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000416; ABJ65282.1; -; Genomic_DNA.
DR   RefSeq; WP_011668803.1; NC_008497.1.
DR   AlphaFoldDB; Q03NE0; -.
DR   SMR; Q03NE0; -.
DR   STRING; 387344.LVIS_2232; -.
DR   ESTHER; lacba-pip; Proline_iminopeptidase.
DR   EnsemblBacteria; ABJ65282; ABJ65282; LVIS_2232.
DR   KEGG; lbr:LVIS_2232; -.
DR   PATRIC; fig|387344.15.peg.2137; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_15_0_9; -.
DR   OMA; TWYRVTG; -.
DR   OrthoDB; 1282004at2; -.
DR   BRENDA; 3.4.11.5; 2851.
DR   Proteomes; UP000001652; 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..299
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000406322"
FT   DOMAIN          29..279
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        245
FT                   /evidence="ECO:0000250|UniProtKB:O32449"
FT   ACT_SITE        272
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P96084"
SQ   SEQUENCE   299 AA;  33711 MW;  D19504D895D360ED CRC64;
     MDIQEEYMPF RAYQTYYRVV GDLRSPLTPL LLLHGGPGST HNYFEAFDQL AMATGRPIVM
     YDQLGCGRSS IPTDPHLWQA ATWVAELRAL RAYLKLDCVH LLGQSWGGML ALIYLCDDQP
     RGIQSVILAS TLSSAHLWAR EQHRLIQFMS TTDQAAIHQA EMTGDFTTPA YLAANERFMI
     QHATGPITEQ TPEFLRRSKR LGTAAYTTAW GPNEYFPTGT LRDYDYTAKL AQLPYPTLVT
     SGVNDLCTPL VAKTMVDQLP HAEWTLFPHS RHMAFIDEPA AYQARLTQWL AAHDEVTDD