ID   PIP_STRCO               Reviewed;         323 AA.
AC   Q9S2L4;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Probable proline iminopeptidase;
DE            Short=PIP;
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase;
DE            Short=PAP;
GN   OrderedLocusNames=SCO1989; ORFNames=SC7H2.03c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939111; CAB52045.1; -; Genomic_DNA.
DR   PIR; T35734; T35734.
DR   RefSeq; NP_626250.1; NC_003888.3.
DR   RefSeq; WP_011028082.1; NZ_VNID01000001.1.
DR   AlphaFoldDB; Q9S2L4; -.
DR   SMR; Q9S2L4; -.
DR   STRING; 100226.SCO1989; -.
DR   ESTHER; strco-SC7H2.03c; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   GeneID; 1097423; -.
DR   KEGG; sco:SCO1989; -.
DR   PATRIC; fig|100226.15.peg.2016; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_043739_2_2_11; -.
DR   InParanoid; Q9S2L4; -.
DR   OMA; YDLLCPP; -.
DR   PhylomeDB; Q9S2L4; -.
DR   Proteomes; UP000001973; 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..323
FT                   /note="Probable proline iminopeptidase"
FT                   /id="PRO_0000080846"
FT   DOMAIN          37..301
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        299
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   323 AA;  35040 MW;  7BEF00133B353EEB CRC64;
     MSLYPEIEPY DHGMLDVGDG NHVYWETCGN PHGKPAVVLH GGPGSRASPG LRRYFDPAAY
     RIVLLDQRGA GRSLPRASAP DTDMSVNTTA HLMADLERLR VHLGIERWLV WGVSWGSVLG
     LRYAQTHPGV VTELVLTGVA TGSNAEVALL TRGLGNIFPE AHERFLAELP PDARDGNLPA
     AYNRLLESPD PAVRERAARA WTDWETATIP APPGSVARYQ DPDFRMGFAR TVTHYWGNDH
     FLGDGNDEGV VIRDAHLLKG IPGTLVQGSL DFGNLLGIVW RLHHAWPDSD LVIVDEAGHD
     AGTTGDEALL AATDKYARGG TAE