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P52279 (PIP_XANCI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proline iminopeptidase

Short name=PIP
EC=3.4.11.5
Alternative name(s):
Prolyl aminopeptidase
Short name=PAP
Gene names
Name:pip
Synonyms:xap
OrganismXanthomonas campestris pv. citri (Xanthomonas citri)
Taxonomic identifier346 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Release of N-terminal proline from a peptide.

Subunit structure

Homooligomer.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase S33 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Proline iminopeptidase
PRO_0000080847

Sites

Active site1101Nucleophile Ref.4
Active site2661 Ref.4
Active site2941Proton donor Ref.4

Experimental info

Sequence conflict951L → V in BAA11623. Ref.3
Sequence conflict121 – 1299ADPSAAGHQ → QTHPQQVTE in BAA11623. Ref.3
Sequence conflict245 – 2517QLLRDAH → SCCATD in BAA11623. Ref.3
Sequence conflict2841Missing in BAA11623. Ref.3

Secondary structure

............................................................. 313
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52279 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 7A9DF2636363FF48

FASTA31335,260
        10         20         30         40         50         60 
MRTLYPEITP YQQGSLKVDD RHTLYFEQCG NPHGKPVVML HGGPGGGCND KMRRFHDPAK 

        70         80         90        100        110        120 
YRIVLFDQRG SGRSTPHADL VDNTTWDLVA DIERLRTHLG VDRWQVFGGS WGSTLALAYA 

       130        140        150        160        170        180 
ADPSAAGHQL VLRGIFLLRR FELEWFYQEG ASRLFPDAWE HYLNAIPPVE RADLMSAFHR 

       190        200        210        220        230        240 
RLTSDDEATR LAAAKAWSVW EGATSFLHVD EDFVTGHEDA HFALAFARIE NHYFVNGGFF 

       250        260        270        280        290        300 
EVEDQLLRDA HRIADIPGVI VHGRYDVVCP LQSAWDLHKA WPKAQLQISP ASGHSAFEPE 

       310 
NVDALVRATD GFA 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z54150 Genomic DNA. Translation: CAA90864.1.
D82882 Genomic DNA. Translation: BAA11623.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZWX-ray2.70A/B1-313[»]
ProteinModelPortalP52279.
SMRP52279. Positions 1-313.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS33.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR002410. Peptidase_S33.
IPR005944. Pro_iminopeptidase.
[Graphical view]
PfamPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFPIRSF006431. Pept_S33. 1 hit.
PRINTSPR00793. PROAMNOPTASE.
SUPFAMSSF53474. SSF53474. 1 hit.
TIGRFAMsTIGR01249. pro_imino_pep_1. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP52279.

Entry information

Entry namePIP_XANCI
AccessionPrimary (citable) accession number: P52279
Secondary accession number(s): P96186
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references