Proline iminopeptidase - Lactobacillus delbrueckii subsp. bulgaricus

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P46544 (PIP_LACDE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Proline iminopeptidase
Short name=PIP
EC=3.4.11.5

Alternative name(s):
Prolyl aminopeptidase
Short name=PAP

Gene names

Name:

pepIP

Organism

Lactobacillus delbrueckii subsp. bulgaricus

Taxonomic identifier

1585 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Releases the N-terminal proline from various substrates. Has a high specificity towards di- or tripeptides with proline at the NH(2)-terminal position, but is not able to hydrolyze longer peptides, or peptides with hydroxyproline at the NH(2)-end. Partially hydrolyzes also peptides with alanine, glycine and leucine at the NH(2)-terminal position. Ref.2
Catalytic activity	Release of N-terminal proline from a peptide. Ref.1 Ref.2 Ref.3
Enzyme regulation	Inhibited strongly by 3,4-dichloroisocoumarin, bestatin and heavy metal ions. Inactivated by p-chloromercuribenzoate, but reactivated by dithiothreitol. Ref.2
Subunit structure	Homotrimer. Ref.2
Subcellular location	Cell envelope Ref.1.
Sequence similarities	Belongs to the peptidase S33 family.
Biophysicochemical properties	Kinetic parameters: K_M=0.93 mM for prolyl-pNA (at 30 degrees Celsius and pH 7.0) Ref.2 Ref.3 V_max=738 mmol/min/mg enzyme with prolyl-pNA as substrate (at 30 degrees Celsius and pH 7.0) pH dependence: Optimum pH is 6-7. Temperature dependence: Stable at temperatures below 40 degrees Celsius.

Ontologies

Keywords
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro envelope Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 295

295

Proline iminopeptidase

PRO_0000080836

Sites

Active site

107

Nucleophile By similarity

Active site

246

By similarity

Active site

273

Proton donor By similarity

Experimental info

Mutagenesis

H → Q: 0.1% of wild-type activity. Ref.3

Mutagenesis

G → D: 0.1% of wild-type activity. Ref.3

Mutagenesis

G → E: Loss of activity. Ref.3

Mutagenesis

P → L: Loss of activity. Ref.3

Mutagenesis

G → D: Loss of activity. Ref.3

Mutagenesis

D → G: Loss of activity. Ref.3

Mutagenesis

G → D: Loss of activity. Ref.3

Mutagenesis

S → F: Loss of activity. Ref.3

Mutagenesis

P → A: 95.4% of wild-type activity. Ref.3

Mutagenesis

E → K: Loss of activity. Ref.3

Mutagenesis

105

G → E: 0.2% of wild-type activity. Ref.3

Mutagenesis

106

Q → L: 21.8% of wild-type activity. KM=0.2 mM for prolyl-pNA. Ref.3

Mutagenesis

107

S → G or N: Loss of activity. Ref.3

Mutagenesis

108

W → Y: 37.9% of wild-type activity. KM=4.0 mM for prolyl-pNA. Ref.3

Mutagenesis

109

G → A: 0.2% of wild-type activity. KM=2.3 mM for prolyl-pNA. Ref.3

Mutagenesis

109

G → S or D: Loss of activity. Ref.3

Mutagenesis

110

G → E: Loss of activity. Ref.3

Mutagenesis

132

S → F: Loss of activity. Ref.3

Mutagenesis

143

E → K: Loss of activity. Ref.3

Mutagenesis

237

P → A: 89.2% of wild-type activity. Ref.3

Mutagenesis

243

G → D: Loss of activity. Ref.3

Mutagenesis

245

D → G: 22.5% of wild-type activity. KM=1.0 mM for prolyl-pNA. Ref.3

Mutagenesis

246

D → G: 0.1% of wild-type activity. KM=1.0 mM for prolyl-pNA. Ref.3

Mutagenesis

273

H → Q: Loss of activity. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P46544 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 97CF3AAD9FAFF900
Show »

FASTA

295

33,027

        10         20         30         40         50         60 
MMQITEKYLP FGNWQTYCRI VGEATDRAPL LLLHGGPGSS HNYFEVLDQV AEKSGRQVIM 

        70         80         90        100        110        120 
YDQLGCGNSS IPDDQAETAY TAQTWVKELE NVREQLGLDQ IHLLGQSWGG MLALIYLCDY 

       130        140        150        160        170        180 
QPEGVKSLIL SSTLASAKLW SQELHRLIKY LPKGEQAAIK EAETTGNYDS LAYQAANAHF 

       190        200        210        220        230        240 
MDQHAIKLTP DLPEPVLRKK KGGSLAYLTG WGPNEYTPIG NLHGYEYTDR LKDLHLPALI 

       250        260        270        280        290 
TSGTDDLCTP LVAKSMYDNL PNARWELFAG CGHMPFVQEN AKYQELLSDW LISQD

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References

[1]	"Cloning, sequencing and characterization of the pepIP gene encoding a proline iminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397." Atlan D., Gilbert C., Blanc B., Portalier R. Microbiology 140:527-535(1994) [PubMed: 8012575] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. Strain: CNRZ 397.
[2]	"Proline iminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397: purification and characterization." Gilbert C., Atlan D., Blanc B., Portalier R. Microbiology 140:537-542(1994) [PubMed: 8012576] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-11, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT. Strain: CNRZ 397.
[3]	"The prolyl aminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus belongs to the alpha/beta hydrolase fold family." Morel F., Gilbert C., Geourjon C., Frot-Coutaz J., Portalier R., Atlan D. Biochim. Biophys. Acta 1429:501-505(1999) [PubMed: 9989236] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CIRCULAR DICHROISM, MUTAGENESIS OF HIS-34; GLY-35; GLY-36; PRO-37; GLY-38; ASP-62; GLY-65; SER-69; PRO-72; GLU-88; GLY-105; GLN-106; SER-107; TRP-108; GLY-109; GLY-110; SER-132; GLU-143; PRO-237; GLY-243; ASP-245; ASP-246 AND HIS-273.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L10712 Genomic DNA. Translation: AAA61596.1.
3D structure databases
ProteinModelPortal	P46544.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR005945. Pept_S33_TRI_F1. IPR002410. Peptidase_S33. [Graphical view]
PIRSF	PIRSF005539. Pept_S33_TRI_F1. 1 hit.
PRINTS	PR00793. PROAMNOPTASE.
TIGRFAMs	TIGR01250. Pro_imino_pep_2. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PIP_LACDE

Accession

Primary (citable) accession number: P46544

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 1, 1996
Last modified:	November 16, 2011
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents