ID   PIP_ELIME               Reviewed;         298 AA.
AC   O05420;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Proline iminopeptidase {ECO:0000250|UniProtKB:P96084};
DE            Short=PIP {ECO:0000250|UniProtKB:P96084};
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000303|PubMed:8951032, ECO:0000312|EMBL:BAA19688.1};
DE            Short=PAP {ECO:0000303|PubMed:8951032};
GN   Name=fpaP;
OS   Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Elizabethkingia.
OX   NCBI_TaxID=238;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAA19688.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=8951032; DOI=10.1006/abbi.1996.0529;
RA   Kitazono A., Kabashima T., Huang H.S., Ito K., Yoshimoto T.;
RT   "Prolyl aminopeptidase gene from Flavobacterium meningosepticum: cloning,
RT   purification of the expressed enzyme, and analysis of its sequence.";
RL   Arch. Biochem. Biophys. 336:35-41(1996).
CC   -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC       Cleaves specifically Pro-betaNA and small peptides containing proline
CC       at the amino terminal. No activity against hydroxyproline-betaNA.
CC       {ECO:0000269|PubMed:8951032}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000269|PubMed:8951032};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH 8.0. {ECO:0000269|PubMed:8951032};
CC       Temperature dependence:
CC         Maximum activity at 42 degrees Celsius. Stable at temperatures up to
CC         44 degrees Celsius, showing 50% of activity after incubation at this
CC         temperature for 15 minutes (at pH 8.0). {ECO:0000269|PubMed:8951032};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8951032}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000255}.
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DR   EMBL; D83254; BAA19688.1; -; Genomic_DNA.
DR   AlphaFoldDB; O05420; -.
DR   SMR; O05420; -.
DR   STRING; 1216967.L100_09504; -.
DR   ESTHER; flame-pamp; Proline_iminopeptidase.
DR   eggNOG; COG2267; Bacteria.
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   1: Evidence at protein level;
KW   Aminopeptidase; Hydrolase; Protease.
FT   CHAIN           1..298
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000406320"
FT   DOMAIN          26..277
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        244
FT                   /evidence="ECO:0000250|UniProtKB:O32449"
FT   ACT_SITE        271
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P96084"
SQ   SEQUENCE   298 AA;  34613 MW;  E5BA17298F949E69 CRC64;
     MIPITTPVGN FKVWTKRFGT NPKIKVLLLH GGPAMTHEYM ECFETFFQRE GFEFYEYDQL
     GSYYSDQPTD EKLWNIDRFV DEVEQVRKAI HADKENFYVL GNSWGGILAM EYALKYQQNL
     KGLIVANMMA SAPEYVKYAE VLSKQMKPEV LAEVRAIEAK KDYANPRYTE LLFPNYYAQH
     ICRLKEWPDA LNRSLKHVNS TVYTLMQGPS ELGMSSDARL AKWDIKNRLH EIATPTLMIG
     ARYDTMDPKA MEEQSKLVQK GRYLYCPNGS HLAMWDDQKV FMDGVIKFIK DVDTKSFN