ID   PIP_NEIMB               Reviewed;         310 AA.
AC   Q9JZR6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=NMB0927;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(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; AE002098; AAF41334.1; -; Genomic_DNA.
DR   PIR; B81141; B81141.
DR   RefSeq; NP_273966.1; NC_003112.2.
DR   RefSeq; WP_002225339.1; NC_003112.2.
DR   AlphaFoldDB; Q9JZR6; -.
DR   SMR; Q9JZR6; -.
DR   STRING; 122586.NMB0927; -.
DR   ESTHER; neigo-pip; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   PaxDb; Q9JZR6; -.
DR   EnsemblBacteria; AAF41334; AAF41334; NMB0927.
DR   KEGG; nme:NMB0927; -.
DR   PATRIC; fig|122586.8.peg.1176; -.
DR   HOGENOM; CLU_043739_2_2_4; -.
DR   OMA; FYQDGAS; -.
DR   Proteomes; UP000000425; 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; Reference proteome.
FT   CHAIN           1..310
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000080843"
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;  34957 MW;  9F883415B1C7B4A2 CRC64;
     MYEIKQPFHS GYLQVSEIHQ IYWEESGNPD GVPVIFLHGG PGAGASPECR GFFNPDVFRI
     VIIDQRGCGR SRPYACAEDN TTWDLVADIE KVREMLGIGK WLVFGGSWGS TLSLAYAQTH
     PERVKGLVLR GIFLCRPSET VWLNEAGGVS RIYPEQWQKF VAPIAENRRN RLIEAYHGLL
     FHQDEEVCLS AAKAWADWES YLIRFEPEEV DEDAYASLAI ARLENHYFVN GGWLQGDRAI
     LNNIGKIRHI PTIIVQGRYD LCTPMQSAWA LSKAFPEAEL RVVQAGHRAF DPPLVDALVQ
     AVEDILPHLL