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P52278 (PIP_LACHE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 67. 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
Synonyms:pepI
OrganismLactobacillus helveticus (Lactobacillus suntoryeus)
Taxonomic identifier1587 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Releases the N-terminal proline from various substrates. Hydrolyzes only di- and tripeptides with proline in the first position. Ref.1

Catalytic activity

Release of N-terminal proline from a peptide. Ref.1

Subunit structure

Homodimer. Ref.1

Subcellular location

Cell envelope Potential.

Sequence similarities

Belongs to the peptidase S33 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.8 mM for Pro-pNA (at 40 degrees Celsius and pH 7.5) Ref.1

Vmax=350 mmol/min/mg enzyme with Pro-pNA as substrate

pH dependence:

Optimum pH is 7.5. At pH values above 7.5, the activity sharply decreases.

Temperature dependence:

Optimum activity at 40 degrees Celsius.

Ontologies

Keywords
   Molecular functionAminopeptidase
Hydrolase
Protease
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

envelope

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 – 294294Proline iminopeptidase
PRO_0000080838

Sites

Active site1051Nucleophile By similarity
Active site2441 By similarity
Active site2711Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P52278 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 535042DAFD636979

FASTA29433,845
        10         20         30         40         50         60 
MEIIEGKMPF MGYETYYRIV GERSEKPPLV LLHGGPGSSH NYFEVLDELA QKDGRRIIMY 

        70         80         90        100        110        120 
DQLGCGESSI PDDHPELYTK ETWVKELEAL REHLALRKMH LLGQSWGGML AIIYMCDYHP 

       130        140        150        160        170        180 
EGIQSLILSS TLSSASLWSK ELHRMIKYLP IEEQAAIHRA ELTGNFNDPD YLKANEHFMN 

       190        200        210        220        230        240 
QHAIDMTKTW PECVMRKKRG GTVAYETAWG PNEYTPEGNL HDYEYTDKLS KIKVPTLITS 

       250        260        270        280        290 
GTDDLCTPYV AKTMQDQIAS SKWRLFEGCG HMSFVEKTDE YVALLQEWLD QHDE 

« Hide

References

[1]"An operon from Lactobacillus helveticus composed of a proline iminopeptidase gene (pepI) and two genes coding for putative members of the ABC transporter family of proteins."
Varmanen P., Rantanen T., Palva A.
Microbiology 142:3459-3468(1996) [PubMed: 9004508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: 53/7.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z56283 Genomic DNA. Translation: CAA91231.1.

3D structure databases

ProteinModelPortalP52278.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005945. Pept_S33_TRI_F1.
IPR002410. Peptidase_S33.
[Graphical view]
PIRSFPIRSF005539. Pept_S33_TRI_F1. 1 hit.
PRINTSPR00793. PROAMNOPTASE.
TIGRFAMsTIGR01250. Pro_imino_pep_2. 1 hit.
ProtoNetSearch...

Entry information

Entry namePIP_LACHE
AccessionPrimary (citable) accession number: P52278
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 16, 2011
This is version 67 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