PIP_XYLFT
ID PIP_XYLFT Reviewed; 313 AA.
AC Q87DF8;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=PD_0727;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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; AE009442; AAO28596.1; -; Genomic_DNA.
DR RefSeq; WP_004088975.1; NC_004556.1.
DR AlphaFoldDB; Q87DF8; -.
DR SMR; Q87DF8; -.
DR ESTHER; xylfa-pip; Proline_iminopeptidase.
DR MEROPS; S33.001; -.
DR EnsemblBacteria; AAO28596; AAO28596; PD_0727.
DR GeneID; 58016274; -.
DR KEGG; xft:PD_0727; -.
DR HOGENOM; CLU_043739_2_2_6; -.
DR OMA; FYQDGAS; -.
DR Proteomes; UP000002516; 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..313
FT /note="Proline iminopeptidase"
FT /id="PRO_0000080849"
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; 35519 MW; 0E2A201E7FA9F0FD CRC64;
MRTLYPEVTP FDHGMLCVDD SHRLYYEQCG NPHGKPVVIL HGGPGGGCND KMRRFHDPDK
YRIVLFDQRG AGRSMPHANL TNNTTWDLVA DIEKLRVALG ITRWQVFGGS WGSTLALAYA
QTHPEQTTEL VLRGIFMLRR WELEWFYQEG ASRLFPDAWD RYIAAIPPVE RHDLISAFHR
RLTSDDEATR LAAAQAWSLW EGATSCLYMD QDFIASHENP HFALAFARIE NHYFVNGGFF
EVEDQLLRDA QRIANIPGVI VHGRYDVVCP LQNAWDLHKA WPKASLKITP GAGHSAFEPQ
NIDALVCATD SFV