ID   PIP_FLAJ1               Reviewed;         297 AA.
AC   A5FIF5;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Proline iminopeptidase {ECO:0000250|UniProtKB:O05420};
DE            Short=PIP {ECO:0000250|UniProtKB:O05420};
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000250|UniProtKB:O05420};
DE            Short=PAP {ECO:0000250|UniProtKB:O05420};
GN   Name=fpaP; OrderedLocusNames=Fjoh_1984;
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX   PubMed=19717629; DOI=10.1128/aem.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
CC   -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC       {ECO:0000250|UniProtKB:O05420}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000250|UniProtKB:O05420};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O05420}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABQ05016.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000685; ABQ05016.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A5FIF5; -.
DR   SMR; A5FIF5; -.
DR   STRING; 376686.Fjoh_1984; -.
DR   ESTHER; flaj1-pip; Proline_iminopeptidase.
DR   EnsemblBacteria; ABQ05016; ABQ05016; Fjoh_1984.
DR   KEGG; fjo:Fjoh_1984; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_15_0_10; -.
DR   Proteomes; UP000006694; Chromosome.
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..297
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000406319"
FT   DOMAIN          26..131
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        243
FT                   /evidence="ECO:0000250|UniProtKB:O32449"
FT   ACT_SITE        270
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P96084"
SQ   SEQUENCE   297 AA;  34609 MW;  0E6199B8B9A7879C CRC64;
     MIPIKTPVGE FKVWIKRFGT NPKIKVLLLH GGPAMTHEYM ECFETFFQRE GFEFYEYDQL
     GSYYSDQPKD SSLWTIDRFV DEVEQVRKAI NADKDNFYVL GNSWGGILAM EYALKYQQNM
     KGLLVSNMMA SAPEYGKYAD EVLAKQMKPE ILKEIRDLEA KKDFENPRYM ELLLPNFYKE
     HLCRLNEWPD GLNRASKHVN GEIYTLMQGP SEFGISGRLA KWDIKNRLHE ITIPTLMIGA
     KYDTMDPKAM EEQSKLVKKG RYLYCPNGSH LAMWDDQKVF MNGVIQFIND VNDEKVN