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P42786 (PIP_NEIGO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismNeisseria gonorrhoeae
Taxonomic identifier485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes peptides having the structure Pro-Y-Z to yield free proline. Also hydrolyzes the dipeptide Pro-Gly.

Catalytic activity

Release of N-terminal proline from a peptide.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the peptidase S33 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical termDirect protein sequencing
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 – 310310Proline iminopeptidase
PRO_0000080841

Sites

Active site1071Nucleophile By similarity
Active site2601 By similarity
Active site2871Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P42786 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: D0E7AEBA908A1AE0

FASTA31034,792
        10         20         30         40         50         60 
MYEIKQPFHS GYLQVSEIHQ IYWEESGNPD GVPVIFLHGG PGAGASPECR GFFNPDVFRI 

        70         80         90        100        110        120 
VIIDQRGCGR SHPYACAEDN TTWDLVADIE KVREMLGIGK WLVFGGSWGS TLSLAYAQTH 

       130        140        150        160        170        180 
PERVKGLVLR GIFLCRPSET AWLNEAGGVS RIYPEQWQKF VAPIAENRRN RLIEAYHGLL 

       190        200        210        220        230        240 
FHQDEEVCLS AAKAWADWES YLIRFEPEGV DEDAYASLAI ARLENHYFVN GGWLQGDKAI 

       250        260        270        280        290        300 
LNNIGKIRHI PTVIVQGRYD LCTPMQSAWE LSKAFPEAEL RVVQAGHCAF DPPLADALVQ 

       310 
AVEDILPRLL 

« Hide

References

[1]"Molecular cloning and characterization of a proline iminopeptidase gene from Neisseria gonorrhoeae."
Albertson N.H., Koomey M.
Mol. Microbiol. 9:1203-1211(1993) [PubMed: 7934933] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
Strain: MS11 / MSO1-1X.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z25461 Genomic DNA. Translation: CAA80948.1.
PIRS39592.

3D structure databases

ProteinModelPortalP42786.
ModBaseSearch...

Protein family/group databases

MEROPSS33.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000073. AB_hydrolase_1.
IPR005944. Pept_S33.
IPR002410. Peptidase_S33.
[Graphical view]
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_NEIGO
AccessionPrimary (citable) accession number: P42786
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 16, 2011
This is version 75 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