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P46542 (PIP_LACDL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 72. 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
Synonyms:pepI
OrganismLactobacillus delbrueckii subsp. lactis
Taxonomic identifier29397 [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. Cleaves Pro-betaNA (L-prolyl-beta-naphthylamide) effectively. Ref.1

Catalytic activity

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

Enzyme regulation

Inhibited by 3,4-DCI, but no significant effect on enzyme activity by pepstatin A, E-64, 1,10-phenanthroline or EDTA. Ref.1

Subunit structure

Homotrimer By similarity.

Subcellular location

Cell envelope Potential.

Sequence similarities

Belongs to the peptidase S33 family.

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_0000080837

Sites

Active site1061Nucleophile By similarity
Active site2451 By similarity
Active site2721Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P46542 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A5E369D34F1620F3

FASTA29432,879
        10         20         30         40         50         60 
MQITEKYLPF GNWQTYCRIV GEATDRAPLL LLHGGPGSSH NYFEVLDQVA EKSGRQVIMY 

        70         80         90        100        110        120 
DQLGCGNSSI PDDQAETAYT AQTWVKELEN VREQLGLDQI HLLGQSWGGM LALIYLCDYQ 

       130        140        150        160        170        180 
PKGVKSLILS STLASAKLWS QELHRLIKYL PKGEQAAIKE AETTGNYDSP AYQAANAHFM 

       190        200        210        220        230        240 
DQHAINVTPD LPEPVLRKKK GGNLAYLTGW GPNEYTPIGN LHGYEYTDRL KDLDLPALIT 

       250        260        270        280        290 
SGTDDLCTPL VAKSMYDHLP NARWELFAGC GHMPFVQENA KYQELLSDWL ISQD 

« Hide

References

[1]"Cloning, heterologous expression, and sequencing of a novel proline iminopeptidase gene, pepI, from Lactobacillus delbrueckii subsp. lactis DSM 7290."
Klein J.R., Schmidt U., Plapp R.
Microbiology 140:1133-1139(1994) [PubMed: 8025678] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
Strain: DSM 7290.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z26948 Genomic DNA. Translation: CAA81556.1.
PIRA59087.

3D structure databases

ProteinModelPortalP46542.
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_LACDL
AccessionPrimary (citable) accession number: P46542
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 16, 2011
This is version 72 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