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P52279

- PIP_XANCI

UniProt

P52279 - PIP_XANCI

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Protein
Proline iminopeptidase
Gene
pip, xap
Organism
Xanthomonas campestris pv. citri (Xanthomonas citri)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in proline metabolism and sensitivity to ascamycin. Has ascamycin dealanylating activity.

Catalytic activityi

Release of N-terminal proline from a peptide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei110 – 1101Nucleophile1 Publication
Active sitei266 – 26611 Publication
Active sitei294 – 2941Proton donor1 Publication

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Protein family/group databases

MEROPSiS33.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline iminopeptidase (EC:3.4.11.5)
Short name:
PIP
Alternative name(s):
Prolyl aminopeptidase
Short name:
PAP
Gene namesi
Name:pip
Synonyms:xap
OrganismiXanthomonas campestris pv. citri (Xanthomonas citri)
Taxonomic identifieri346 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Proline iminopeptidase
PRO_0000080847Add
BLAST

Interactioni

Subunit structurei

Homooligomer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 177
Beta strandi19 – 213
Beta strandi23 – 308
Beta strandi34 – 407
Turni43 – 464
Helixi50 – 556
Turni58 – 603
Beta strandi61 – 666
Beta strandi74 – 763
Helixi85 – 9814
Beta strandi102 – 1098
Helixi111 – 12212
Helixi124 – 1263
Beta strandi127 – 1348
Helixi140 – 1478
Helixi151 – 1544
Helixi156 – 1649
Helixi168 – 1703
Helixi174 – 1829
Helixi187 – 20317
Beta strandi205 – 2084
Helixi211 – 2177
Helixi220 – 23516
Helixi237 – 2393
Helixi245 – 2484
Helixi250 – 2534
Beta strandi258 – 2636
Beta strandi267 – 2693
Helixi271 – 28010
Beta strandi284 – 2896
Helixi299 – 31214

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZWX-ray2.70A/B1-313[»]
ProteinModelPortaliP52279.
SMRiP52279. Positions 1-313.

Miscellaneous databases

EvolutionaryTraceiP52279.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S33 family.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR002410. Peptidase_S33.
IPR005944. Pro_iminopeptidase.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006431. Pept_S33. 1 hit.
PRINTSiPR00793. PROAMNOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01249. pro_imino_pep_1. 1 hit.

Sequencei

Sequence statusi: Complete.

P52279-1 [UniParc]FASTAAdd to Basket

« Hide

MRTLYPEITP YQQGSLKVDD RHTLYFEQCG NPHGKPVVML HGGPGGGCND    50
KMRRFHDPAK YRIVLFDQRG SGRSTPHADL VDNTTWDLVA DIERLRTHLG 100
VDRWQVFGGS WGSTLALAYA ADPSAAGHQL VLRGIFLLRR FELEWFYQEG 150
ASRLFPDAWE HYLNAIPPVE RADLMSAFHR RLTSDDEATR LAAAKAWSVW 200
EGATSFLHVD EDFVTGHEDA HFALAFARIE NHYFVNGGFF EVEDQLLRDA 250
HRIADIPGVI VHGRYDVVCP LQSAWDLHKA WPKAQLQISP ASGHSAFEPE 300
NVDALVRATD GFA 313
Length:313
Mass (Da):35,260
Last modified:November 1, 1997 - v2
Checksum:i7A9DF2636363FF48
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951L → V in BAA11623. 1 Publication
Sequence conflicti121 – 1299ADPSAAGHQ → QTHPQQVTE in BAA11623. 1 Publication
Sequence conflicti245 – 2517QLLRDAH → SCCATD in BAA11623. 1 Publication
Sequence conflicti284 – 2841Missing in BAA11623. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z54150 Genomic DNA. Translation: CAA90864.1.
D82882 Genomic DNA. Translation: BAA11623.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z54150 Genomic DNA. Translation: CAA90864.1 .
D82882 Genomic DNA. Translation: BAA11623.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AZW X-ray 2.70 A/B 1-313 [» ]
ProteinModelPortali P52279.
SMRi P52279. Positions 1-313.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S33.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P52279.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR002410. Peptidase_S33.
IPR005944. Pro_iminopeptidase.
[Graphical view ]
Pfami PF00561. Abhydrolase_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF006431. Pept_S33. 1 hit.
PRINTSi PR00793. PROAMNOPTASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
TIGRFAMsi TIGR01249. pro_imino_pep_1. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Proline iminopeptidase gene from Xanthomonas campestris pv. citri."
    Alonso J., Garcia J.L.
    Microbiology 142:2951-2957(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NBRC 3835.
  2. Alonso J.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Isolation and characterization of the gene encoding an aminopeptidase involved in the selective toxicity of ascamycin toward Xanthomonas campestris pv. citri."
    Sudo T., Shinohara K., Dohmae N., Takio K., Usami R., Horikoshi K., Osada H.
    Biochem. J. 319:99-102(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20 AND 283-296.
    Strain: NBRC 3781.
  4. "Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family."
    Medrano F.J., Alonso J., Garcia J.L., Romero A., Bode W., Gomis-Ruth F.X.
    EMBO J. 17:1-9(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), ACTIVE SITE.

Entry informationi

Entry nameiPIP_XANCI
AccessioniPrimary (citable) accession number: P52279
Secondary accession number(s): P96186
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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