ID   PIP_MYCPN               Reviewed;         309 AA.
AC   P75092;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Putative proline iminopeptidase;
DE            Short=PIP;
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase;
DE            Short=PAP;
GN   Name=pip; OrderedLocusNames=MPN_022; ORFNames=MP132;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB95780.1; -; Genomic_DNA.
DR   PIR; S73458; S73458.
DR   RefSeq; NP_109710.1; NC_000912.1.
DR   RefSeq; WP_010874379.1; NC_000912.1.
DR   AlphaFoldDB; P75092; -.
DR   SMR; P75092; -.
DR   IntAct; P75092; 4.
DR   STRING; 272634.MPN_022; -.
DR   ESTHER; mycpn-pip; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   EnsemblBacteria; AAB95780; AAB95780; MPN_022.
DR   GeneID; 66609337; -.
DR   KEGG; mpn:MPN_022; -.
DR   PATRIC; fig|272634.6.peg.21; -.
DR   HOGENOM; CLU_043739_2_2_14; -.
DR   OMA; FYQDGAS; -.
DR   BioCyc; MPNE272634:G1GJ3-33-MON; -.
DR   Proteomes; UP000000808; Chromosome.
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; Reference proteome.
FT   CHAIN           1..309
FT                   /note="Putative proline iminopeptidase"
FT                   /id="PRO_0000080840"
FT   DOMAIN          33..291
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        105
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  34690 MW;  6E414919FC01E767 CRC64;
     MNTSPKQSGY LKVGNGHEVY FWTAGNPQGK SALYVHGGPG SGTDAGCLKY FDLDTTYVIL
     LDQRGCGQSK AVNPLLHNTT QDLVGDLEAL RQHLKLERWT LFGGSWGSTL ALVYAITHPQ
     VVEQVFLRAL FLGREQDWAE MLLGLGKLFY PYEHQTLLKA IPQACRTDFT KFTNYFYEVL
     QGNDSALKTQ LANAWVKWEN TLLSPISYVK DEKAEDANFT FKLALLECHY AKHHSFLKPN
     FILENVAVLK DKPVHLIHGR FDLVCPLSQA LELKRALPTL NLYVTNNAGH SGSDPNNLTT
     IKHLLKTQL