ID   PIP_NEIMA               Reviewed;         310 AA.
AC   Q9JUV1; A1IRE4;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Proline iminopeptidase;
DE            Short=PIP;
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase;
DE            Short=PAP;
GN   Name=pip; OrderedLocusNames=NMA1122;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM08330.1; -; Genomic_DNA.
DR   PIR; F81878; F81878.
DR   RefSeq; WP_002246883.1; NC_003116.1.
DR   AlphaFoldDB; Q9JUV1; -.
DR   SMR; Q9JUV1; -.
DR   ESTHER; neigo-pip; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   PRIDE; Q9JUV1; -.
DR   EnsemblBacteria; CAM08330; CAM08330; NMA1122.
DR   KEGG; nma:NMA1122; -.
DR   HOGENOM; CLU_043739_2_2_4; -.
DR   OMA; FYQDGAS; -.
DR   BioCyc; NMEN122587:NMA_RS05635-MON; -.
DR   Proteomes; UP000000626; 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; PR00111; ABHYDROLASE.
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.
FT   CHAIN           1..310
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000080842"
FT   DOMAIN          33..290
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        260
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        287
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  34901 MW;  9F888B54135478A1 CRC64;
     MYEIKQPFHS GYLQVSEIHQ IYWEESGNPD GVPVIFLHGG PGAGASPECR GFFNPDVFRI
     VIIDQRGCGR SRPYACAEDN TTWDLVADIE KVREMLGIGK WLVFGGSWGS TLSLAYAQTH
     PERVKGLVLR GIFLCRPSET VWLNEAGGVS RIYPEQWQKF VAPIAENRRN QLIEAYHGLL
     FHQDEEVCLS AAKAWADWES YLIRFEPEEV DEDAYASLAI ARLENHYFVN GGWLQGDRAI
     LNNIGKIQHI PTIIVQGRYD LCTPMQSAWA LSKAFPEAEL RVVQAGHRAF DPPLVDALVQ
     AVEDILPHLL