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Q9PD69 (PIP_XYLFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:XF_1510
OrganismXylella fastidiosa [Complete proteome] [HAMAP]
Taxonomic identifier2371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Specifically catalyzes the removal of N-terminal proline residues from peptides By similarity.

Catalytic activity

Release of N-terminal proline from a peptide.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase S33 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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_0000080848

Sites

Active site1101Nucleophile By similarity
Active site2661 By similarity
Active site2941Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PD69 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7A351C54DEF11636

FASTA31335,592
        10         20         30         40         50         60 
MRTLYPEVTP FEHGILCVDD NHRLYYEQCG NPHGKPVVIL HGGPGSGCND KMRRFHDPDK 

        70         80         90        100        110        120 
YRIVLFDQRG AGRSTPHANL TNNTTWDLVA DIEKLRVALG ITRWQVFGGS WGSTLALAYA 

       130        140        150        160        170        180 
QTHPEQTTEL VLRGIFMLRR WELEWFYQEG ASHLFPDAWD RYIAVIPPVE RHDLISAFHR 

       190        200        210        220        230        240 
RLTSEDEATR LAAAQAWSLW EGATSCLYMD QDFIASHENP HFALAFARIE NHYFVNGGFF 

       250        260        270        280        290        300 
EVENQLLRDA QRIANIPGVI VHGRYDVVCP LQNAWDLHKV WPKASLKITP GAGHSAFEPQ 

       310 
NIDALVCATD SFV

« Hide

References

[1]"The genome sequence of the plant pathogen Xylella fastidiosa."
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. expand/collapse author list , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
Nature 406:151-159(2000) [PubMed: 10910347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9a5c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003849 Genomic DNA. Translation: AAF84319.1.
PIRE82671.
RefSeqNP_298799.1. NC_002488.3.

3D structure databases

ProteinModelPortalQ9PD69.
SMRQ9PD69. Positions 1-312.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1127056.
GenomeReviewsGene locus XF_1510 in contig AE003849_GR.
KEGGxfa:XF1510.
NMPDRfig|160492.1.peg.1506.
PATRIC24133132. VBIXylFas578_1594.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG677789.
OMAAELDWYY.
ProtClustDBCLSK446283.

Enzyme and pathway databases

BioCycXFAS160492:XF1510-MONOMER.

Family and domain databases

InterProIPR000073. AB_hydrolase_1.
IPR005944. Pept_S33.
IPR002410. Peptidase_S33.
[Graphical view]
KOK01259.
PANTHERPTHR10992:SF12. PTHR10992:SF12. 1 hit.
PfamPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFPIRSF006431. Pept_S33. 1 hit.
PRINTSPR00111. ABHYDROLASE.
PR00793. PROAMNOPTASE.
TIGRFAMsTIGR01249. Pro_imino_pep_1. 1 hit.
ProtoNetSearch...

Entry information

Entry namePIP_XYLFA
AccessionPrimary (citable) accession number: Q9PD69
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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