ID PIP_XANCI Reviewed; 313 AA. AC P52279; P96186; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-SEP-2023, 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; Synonyms=xap; OS Xanthomonas citri (Xanthomonas campestris pv. citri). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=346; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NBRC 3835; RX PubMed=8885412; DOI=10.1099/13500872-142-10-2951; RA Alonso J., Garcia J.L.; RT "Proline iminopeptidase gene from Xanthomonas campestris pv. citri."; RL Microbiology 142:2951-2957(1996). RN [2] RP SEQUENCE REVISION. RA Alonso J.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20 AND RP 283-296. RC STRAIN=NBRC 3781; RX PubMed=8870654; DOI=10.1042/bj3190099; RA Sudo T., Shinohara K., Dohmae N., Takio K., Usami R., Horikoshi K., RA Osada H.; RT "Isolation and characterization of the gene encoding an aminopeptidase RT involved in the selective toxicity of ascamycin toward Xanthomonas RT campestris pv. citri."; RL Biochem. J. 319:99-102(1996). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND ACTIVE SITE. RX PubMed=9427736; DOI=10.1093/emboj/17.1.1; RA Medrano F.J., Alonso J., Garcia J.L., Romero A., Bode W., Gomis-Ruth F.X.; RT "Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: RT a prototype for the prolyl oligopeptidase family."; RL EMBO J. 17:1-9(1998). CC -!- FUNCTION: May be involved in proline metabolism and sensitivity to CC ascamycin. Has ascamycin dealanylating activity. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; CC -!- SUBUNIT: Homooligomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z54150; CAA90864.1; -; Genomic_DNA. DR EMBL; D82882; BAA11623.1; -; Genomic_DNA. DR PDB; 1AZW; X-ray; 2.70 A; A/B=1-313. DR PDBsum; 1AZW; -. DR AlphaFoldDB; P52279; -. DR SMR; P52279; -. DR ESTHER; xanca-impep; Proline_iminopeptidase. DR MEROPS; S33.001; -. DR EvolutionaryTrace; P52279; -. 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; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR002410; Peptidase_S33. DR InterPro; IPR005944; Pro_iminopeptidase. DR NCBIfam; TIGR01249; pro_imino_pep_1; 1. DR PANTHER; PTHR43722; PROLINE IMINOPEPTIDASE; 1. DR PANTHER; PTHR43722:SF1; PROLINE IMINOPEPTIDASE; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR PIRSF; PIRSF006431; Pept_S33; 1. DR PRINTS; PR00793; PROAMNOPTASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminopeptidase; Cytoplasm; Direct protein sequencing; KW Hydrolase; Protease. FT CHAIN 1..313 FT /note="Proline iminopeptidase" FT /id="PRO_0000080847" FT DOMAIN 35..298 FT /note="AB hydrolase-1" FT /evidence="ECO:0000255" FT ACT_SITE 110 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:9427736" FT ACT_SITE 266 FT /evidence="ECO:0000269|PubMed:9427736" FT ACT_SITE 294 FT /note="Proton donor" FT /evidence="ECO:0000269|PubMed:9427736" FT CONFLICT 95 FT /note="L -> V (in Ref. 3; BAA11623)" FT /evidence="ECO:0000305" FT CONFLICT 121..129 FT /note="ADPSAAGHQ -> QTHPQQVTE (in Ref. 3; BAA11623)" FT /evidence="ECO:0000305" FT CONFLICT 245..251 FT /note="QLLRDAH -> SCCATD (in Ref. 3; BAA11623)" FT /evidence="ECO:0000305" FT CONFLICT 284 FT /note="Missing (in Ref. 3; BAA11623)" FT /evidence="ECO:0000305" FT STRAND 11..17 FT /evidence="ECO:0007829|PDB:1AZW" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:1AZW" FT STRAND 23..30 FT /evidence="ECO:0007829|PDB:1AZW" FT STRAND 34..40 FT /evidence="ECO:0007829|PDB:1AZW" FT TURN 43..46 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 50..55 FT /evidence="ECO:0007829|PDB:1AZW" FT TURN 58..60 FT /evidence="ECO:0007829|PDB:1AZW" FT STRAND 61..66 FT /evidence="ECO:0007829|PDB:1AZW" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 85..98 FT /evidence="ECO:0007829|PDB:1AZW" FT STRAND 102..109 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 111..122 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:1AZW" FT STRAND 127..134 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 140..147 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 151..154 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 156..164 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 174..182 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 187..203 FT /evidence="ECO:0007829|PDB:1AZW" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 211..217 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 220..235 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 237..239 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 245..248 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 250..253 FT /evidence="ECO:0007829|PDB:1AZW" FT STRAND 258..263 FT /evidence="ECO:0007829|PDB:1AZW" FT STRAND 267..269 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 271..280 FT /evidence="ECO:0007829|PDB:1AZW" FT STRAND 284..289 FT /evidence="ECO:0007829|PDB:1AZW" FT HELIX 299..312 FT /evidence="ECO:0007829|PDB:1AZW" SQ SEQUENCE 313 AA; 35260 MW; 7A9DF2636363FF48 CRC64; MRTLYPEITP YQQGSLKVDD RHTLYFEQCG NPHGKPVVML HGGPGGGCND KMRRFHDPAK YRIVLFDQRG SGRSTPHADL VDNTTWDLVA DIERLRTHLG VDRWQVFGGS WGSTLALAYA ADPSAAGHQL VLRGIFLLRR FELEWFYQEG ASRLFPDAWE HYLNAIPPVE RADLMSAFHR RLTSDDEATR LAAAKAWSVW EGATSFLHVD EDFVTGHEDA HFALAFARIE NHYFVNGGFF EVEDQLLRDA HRIADIPGVI VHGRYDVVCP LQSAWDLHKA WPKAQLQISP ASGHSAFEPE NVDALVRATD GFA //