ID   PIP_AERSO               Reviewed;         425 AA.
AC   P46547;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Proline iminopeptidase;
DE            Short=PIP;
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase;
DE            Short=PAP;
GN   Name=pip; Synonyms=pap;
OS   Aeromonas sobria.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7883756; DOI=10.1093/oxfordjournals.jbchem.a124601;
RA   Kitazono A., Kitano A., Tsuru D., Yoshimoto T.;
RT   "Isolation and characterization of the prolyl aminopeptidase gene (pap)
RT   from Aeromonas sobria: comparison with the Bacillus coagulans enzyme.";
RL   J. Biochem. 116:818-825(1994).
CC   -!- FUNCTION: Higher activity toward long peptides. Acts on hydroxyproline
CC       beta-naphthylamide with almost as high an activity as on proline beta-
CC       naphthylamide.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; D30714; BAA06380.1; -; Genomic_DNA.
DR   PIR; JC4184; JC4184.
DR   AlphaFoldDB; P46547; -.
DR   SMR; P46547; -.
DR   ESTHER; aerso-pip; Proline_iminopeptidase.
DR   MEROPS; S33.008; -.
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   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 2.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cytoplasm; Direct protein sequencing; Hydrolase; Protease.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..425
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000080834"
FT   DOMAIN          52..315
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        146
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        351
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        404
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   425 AA;  48406 MW;  774F14CC3F797F28 CRC64;
     MSSPLHYVLD GIHCEPHFFT VPLDHQQPDD EETITLFGRT LCRKDRLDDE LPWLLYLQGG
     PGFGAPRPSA NGGWIKRALQ EFRVLLLDQR GTGHSTPIHA ELLAHLNPRQ QADYLSHFRA
     DSIVRDAELI REQLSPDHPW SLLGQSFGGF CSLTYLSLFP DSLHEVYLTG GVAPIGRSAD
     EVYRATYQRV ADKNRAFFAR FPHAQAIANR LATHLQRHDV RLPNGQRLTV EQLQQQGLDL
     GASGAFEELY YLLEDAFIGE KLNPAFLYQV QAMQPFNTNP VFAILHELIY CEGAASHWAA
     ERVRGEFPAL AWAQGKDFAF TGEMIFPWMF EQFRELIPLK EAAHLLAEKA DWGPLYDPVQ
     LARNKVPVAC AVYAEDMYVE FDYSRETLKG LSNSRAWITN EYEHNGLRVD GEQILDRLIR
     LNRDC