PIP_XANCI
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 03-AUG-2022, entry version 99.
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; Proteobacteria; 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}.
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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; -; 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; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01249; pro_imino_pep_1; 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
