ID   PIP_LEPBY               Reviewed;         321 AA.
AC   O83041;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Probable proline iminopeptidase;
DE            Short=PIP;
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase;
DE            Short=PAP;
GN   Name=pip;
OS   Leptolyngbya boryana (Plectonema boryanum).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Leptolyngbyaceae; Leptolyngbya.
OX   NCBI_TaxID=1184;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DG5;
RA   Matsumura T., Fujita Y., Hase T.;
RT   "Cyanobacterial ferredoxin gene.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically catalyzes the removal of N-terminal proline
CC       residues from peptides. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; AB017194; BAA32603.1; -; Genomic_DNA.
DR   AlphaFoldDB; O83041; -.
DR   SMR; O83041; -.
DR   ESTHER; plebo-pip; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   GO; GO:0005737; C:cytoplasm; 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; IPR005944; Pro_iminopeptidase.
DR   PANTHER; PTHR43722; PTHR43722; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF006431; Pept_S33; 1.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01249; pro_imino_pep_1; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Protease.
FT   CHAIN           1..321
FT                   /note="Probable proline iminopeptidase"
FT                   /id="PRO_0000080844"
FT   DOMAIN          35..296
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        110
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        294
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  36475 MW;  94EF1D7D62F5841E CRC64;
     MRQLYPAIAP YQSGMLPVSA LHTIYYEQSG NPNGKPVVFL HGGPGGGTIP TYRQYFDPSK
     WRIILFDQRG AGKSTPHAEL RENTTWDLVS DIEKLRSHLN IDRWFVFGGS WGSTLSLAYS
     QTHPDRCLGL ILRGIFLLRR KEILWFYQDG ASWIFPDAWE HYLEPIPPEE RDDMISAYYR
     RLTSKDAEIR STAAKAWSVW EGTTSRLIVD PSLQSKFADD EFADAFARIE CHYFINRGFF
     ETDDQLLQNC DRIAHIPTVI VQGRYDVVCP MTSAWALHKA LPESELIVVP DAGHSMMEAG
     ILSALIDATD RFVAQKTNGK I