Reviewed, UniProtKB/Swiss-Prot P46544 (PIP_LACDE)

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.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Characterized by 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.
Catalytic activity	Release of N-terminal proline from a peptide.
Subunit structure	Homotrimer.
Subcellular location	Cell envelope.
Sequence similarities	Belongs to the peptidase S33 family.

Ontologies

Keywords
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
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	1	Nucleophile By similarity
	Active site	246	1	By similarity
	Active site	273	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P46544-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 97CF3AAD9FAFF900	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

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]. 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, CHARACTERIZATION. Strain: CNRZ 397.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L10712 Genomic DNA. Translation: AAA61596.1.
3D structure databases
HSSP	HSSP built from PDB template 1MTZ based on UniProtKB P96084.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.4.11.5. 278872.
Family and domain databases
InterPro	IPR000073. AB_hydrolase_1. IPR005945. Pept_S33_TRI_F1. IPR002410. Peptidase_S33. [Graphical view]
Pfam	PF00561. Abhydrolase_1. 1 hit. [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:	June 16, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)