ID   PIP_XYLFA               Reviewed;         313 AA.
AC   Q9PD69;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=XF_1510;
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=160492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c;
RX   PubMed=10910347; DOI=10.1038/35018003;
RA   Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA   Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA   Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA   Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA   Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA   Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA   Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA   Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA   Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA   Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA   Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA   Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA   Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA   Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA   Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA   Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA   de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA   Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA   Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA   Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA   da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA   Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA   Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA   Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT   "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL   Nature 406:151-159(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; AE003849; AAF84319.1; -; Genomic_DNA.
DR   PIR; E82671; E82671.
DR   RefSeq; WP_010894011.1; NC_002488.3.
DR   AlphaFoldDB; Q9PD69; -.
DR   SMR; Q9PD69; -.
DR   STRING; 160492.XF_1510; -.
DR   ESTHER; xylfa-pip; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   EnsemblBacteria; AAF84319; AAF84319; XF_1510.
DR   KEGG; xfa:XF_1510; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_043739_2_2_6; -.
DR   OMA; FYQDGAS; -.
DR   Proteomes; UP000000812; 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..313
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000080848"
FT   DOMAIN          35..298
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        110
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        294
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  35592 MW;  7A351C54DEF11636 CRC64;
     MRTLYPEVTP FEHGILCVDD NHRLYYEQCG NPHGKPVVIL HGGPGSGCND KMRRFHDPDK
     YRIVLFDQRG AGRSTPHANL TNNTTWDLVA DIEKLRVALG ITRWQVFGGS WGSTLALAYA
     QTHPEQTTEL VLRGIFMLRR WELEWFYQEG ASHLFPDAWD RYIAVIPPVE RHDLISAFHR
     RLTSEDEATR LAAAQAWSLW EGATSCLYMD QDFIASHENP HFALAFARIE NHYFVNGGFF
     EVENQLLRDA QRIANIPGVI VHGRYDVVCP LQNAWDLHKV WPKASLKITP GAGHSAFEPQ
     NIDALVCATD SFV