ID   PIP_BREBN               Reviewed;         292 AA.
AC   C0ZKI1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Proline iminopeptidase {ECO:0000312|EMBL:BAH45658.1};
DE            Short=PIP {ECO:0000250|UniProtKB:P46541};
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000250|UniProtKB:P46541};
DE            Short=PAP {ECO:0000250|UniProtKB:P46541};
GN   Name=pip {ECO:0000312|EMBL:BAH45658.1}; OrderedLocusNames=BBR47_46810;
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=358681;
RN   [1] {ECO:0000312|EMBL:BAH45658.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599;
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000250|UniProtKB:P46541};
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP008955; BAH45658.1; -; Genomic_DNA.
DR   RefSeq; WP_015892919.1; NC_012491.1.
DR   AlphaFoldDB; C0ZKI1; -.
DR   SMR; C0ZKI1; -.
DR   STRING; 358681.BBR47_46810; -.
DR   ESTHER; brebn-pip; Proline_iminopeptidase.
DR   EnsemblBacteria; BAH45658; BAH45658; BBR47_46810.
DR   KEGG; bbe:BBR47_46810; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_15_0_9; -.
DR   OMA; TWYRVTG; -.
DR   OrthoDB; 1282004at2; -.
DR   Proteomes; UP000001877; 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; Reference proteome.
FT   CHAIN           1..292
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000406316"
FT   DOMAIN          27..274
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        102
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P96084"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000250|UniProtKB:O32449"
FT   ACT_SITE        268
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P96084"
SQ   SEQUENCE   292 AA;  33277 MW;  EA2424D31DAD2000 CRC64;
     MRMQEGYIEV PGGRVWYSRV GEGEKTPLIV LHGGPGNTHD PLKSTLHVLG DDRPVIFYDQ
     LGSGNSDRPT DLTLWKTERF VEELACIRQA LDLKEVHILG HSWGTMLAAA YLVDAKPEGV
     QSIIFSSPCL SAERWKQDAD RLIEQLPVDT QQTIATHEEQ GTTDSQEYQD AMKEYYKRHV
     CRLDPMPTVM TESRPKANKE VYMTMWGPSE FCPTGNLKTF DYTPQLHQIN IPSLFVCGRY
     DEATPESTGY YQSLVPKAEL HVFENSSHVG YLEETDEYVQ VIRRFLQKAE SK