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O07883 (PCP_THELI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
Gene names
Name:pcp
OrganismThermococcus litoralis
Taxonomic identifier2265 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP MF_00417.

Sequence similarities

Belongs to the peptidase C15 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Pyrrolidone-carboxylate peptidase HAMAP MF_00417
PRO_0000184760

Sites

Active site801
Active site1431
Active site1671

Amino acid modifications

Disulfide bond190Interchain HAMAP MF_00417

Secondary structure

1 ................................. 220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O07883 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 58B9774015D07ADC

FASTA22024,747
        10         20         30         40         50         60 
MKKVLITGFE PFGGDSKNPT EQIAKYFDRK QIGNAMVYGR VLPVSVKRAT IELKRYLEEI 

        70         80         90        100        110        120 
KPEIVINLGL APTYSNITVE RIAVNIIDAR IPDNDGYQPI DEKIEEDAPL AYMATLPVRA 

       130        140        150        160        170        180 
ITKTLRDNGI PATISYSAGT YLCNYVMFKT LHFSKIEGYP LKAGFIHVPY TPDQVVNKFF 

       190        200        210        220 
LLGKNTPSMC LEAEIKAIEL AVKVSLDYLE KDRDDIKIPL

« Hide

References

[1]"Cloning, expression, and characterization of pyrrolidone carboxyl peptidase from the archaeon Thermococcus litoralis."
Singleton M.R., Taylor S.J.C., Parrat J.S., Littlechild J.A.
Extremophiles 4:297-303(2000) [PubMed: 11057915] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: NS-C.
[2]"Crystallization and preliminary X-ray diffraction studies of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis."
Singleton M.R., Isupov M.N., Littlechild J.A.
Acta Crystallogr. D 55:702-703(1999) [PubMed: 10089475] [Abstract]
Cited for: CRYSTALLIZATION.
[3]"X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis."
Singleton M.R., Isupov M.N., Littlechild J.A.
Structure 7:237-244(1999) [PubMed: 10368293] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y13966 Genomic DNA. Translation: CAA74299.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2ZX-ray1.73A/B/C/D1-220[»]
ProteinModelPortalO07883.
SMRO07883. Positions 1-220.
ModBaseSearch...

Protein family/group databases

MEROPSC15.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00417. Pyrrolid_peptidase.
[Tree]
InterProIPR000816. Peptidase_C15.
IPR016125. Peptidase_C15-like.
[Graphical view]
Gene3DG3DSA:3.40.630.20. Peptidase_C15-like. 1 hit.
PANTHERPTHR23402. Peptidase_C15-like. 1 hit.
PfamPF01470. Peptidase_C15. 1 hit.
[Graphical view]
PIRSFPIRSF015592. Prld-crbxl_pptds. 1 hit.
PRINTSPR00706. PYROGLUPTASE.
SUPFAMSSF53182. Peptidase_C15-like. 1 hit.
TIGRFAMsTIGR00504. Pyro_pdase. 1 hit.
PROSITEPS01334. PYRASE_CYS. 1 hit.
PS01333. PYRASE_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePCP_THELI
AccessionPrimary (citable) accession number: O07883
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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