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O87765 (PCP_LACLM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. 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:
Pyrrolidone-carboxylate peptidase

EC=3.4.19.3
Alternative name(s):
5-oxoprolyl-peptidase
Pyroglutamyl-peptidase I
Short name=PGP-I
Short name=Pyrase
Gene names
Name:pcp
Ordered Locus Names:llmg_0663
OrganismLactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]
Taxonomic identifier416870 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Removes 5-oxoproline from various penultimate amino acid residues except L-proline By similarity. HAMAP-Rule MF_00417

Catalytic activity

Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro. HAMAP-Rule MF_00417

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00417

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00417.

Sequence similarities

Belongs to the peptidase C15 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

pyroglutamyl-peptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Pyrrolidone-carboxylate peptidase HAMAP-Rule MF_00417
PRO_0000184722

Sites

Active site781 By similarity
Active site1411 By similarity
Active site1651 By similarity

Sequences

Sequence LengthMass (Da)Tools
O87765 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 70AE7E36E0882289

FASTA21523,519
        10         20         30         40         50         60 
MKILVTGFDP FGDDKINPAI EAVKRLPDEI AGAQIVKLEI PTKFNVSADV VKDAIAKEKP 

        70         80         90        100        110        120 
DYVLSIGQAG GRFELTPERV AINLDDGRIQ DNAGYQPLNH TIHGDDENAY FTQLPIKAMA 

       130        140        150        160        170        180 
KAIREAGVPS AVSNTAGTYV CNHIFYQVQY MRDKMFPDIK AGFMHIPFLP EQVVTRPETP 

       190        200        210 
ALSLDDDVLG ITAAIKAIVS RDGKGDIETI EGKDH 

« Hide

References

« Hide 'large scale' references
[1]"A natural large chromosomal inversion in Lactococcus lactis is mediated by homologous recombination between two insertion sequences."
Daveran-Mingot M.L., Campo N., Ritzenthaler P., le Bourgeois P.
J. Bacteriol. 180:4834-4842(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Pyrrolidone carboxyl peptidase of Lactococcus lactis MG1363."
Buist G., Haandrikman A.J., Benus G., Feenstra B., Venema G., Kok J.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363."
Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.
J. Bacteriol. 189:3256-3270(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MG1363.
[4]"Identification and characterisation of a gene encoding aminoacylase activity from Lactococcus lactis MG1363."
Curley P., van Sinderen D.
FEMS Microbiol. Lett. 183:177-182(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-215.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ223960 Genomic DNA. Translation: CAA11691.1.
AJ223962 Genomic DNA. Translation: CAA11699.1.
AF323462 Genomic DNA. Translation: AAK20299.1.
AM406671 Genomic DNA. Translation: CAL97264.1.
AF168363 Genomic DNA. Translation: AAF36226.1.
RefSeqYP_001032004.1. NC_009004.1.

3D structure databases

ProteinModelPortalO87765.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING416870.llmg_0663.

Protein family/group databases

MEROPSC15.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL97264; CAL97264; llmg_0663.
GeneID4797823.
KEGGllm:llmg_0663.
PATRIC22282430. VBILacLac4574_0679.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2039.
HOGENOMHOG000242641.
KOK01304.
OMAKPNTPSM.
OrthoDBEOG6X1124.

Enzyme and pathway databases

BioCycLLAC416870:GCDT-693-MONOMER.

Family and domain databases

Gene3D3.40.630.20. 1 hit.
HAMAPMF_00417. Pyrrolid_peptidase.
InterProIPR000816. Peptidase_C15.
IPR016125. Peptidase_C15-like.
[Graphical view]
PANTHERPTHR23402. PTHR23402. 1 hit.
PfamPF01470. Peptidase_C15. 1 hit.
[Graphical view]
PIRSFPIRSF015592. Prld-crbxl_pptds. 1 hit.
PRINTSPR00706. PYROGLUPTASE.
SUPFAMSSF53182. SSF53182. 1 hit.
TIGRFAMsTIGR00504. pyro_pdase. 1 hit.
PROSITEPS01334. PYRASE_CYS. 1 hit.
PS01333. PYRASE_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePCP_LACLM
AccessionPrimary (citable) accession number: O87765
Secondary accession number(s): A2RJ15, Q9L9P5, Q9R805
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: May 14, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries