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B7IEE2 (PCP_THEAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 36. 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:THA_1947
OrganismThermosipho africanus (strain TCF52B) [Complete proteome] [HAMAP]
Taxonomic identifier484019 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermosipho

Protein attributes

Sequence length205 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 – 205205Pyrrolidone-carboxylate peptidase HAMAP-Rule MF_00417
PRO_1000124004

Sites

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

Sequences

Sequence LengthMass (Da)Tools
B7IEE2 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 3D6E8BC7E2F10FD2

FASTA20522,818
        10         20         30         40         50         60 
MKILITGFEP FGGEVVNPSF EAVKHLPDSI EKAQIVKAAI HTVFRKSIEV LEELIVKEKP 

        70         80         90        100        110        120 
DIVICVGQAG GRAEITIERV AINIDDAKNP DNEGNTPKDE VIFEDGENAY FSNLPIKKMV 

       130        140        150        160        170        180 
EEIKNCKIPA SISNSAGTYV CNHLMYGLLY LINKKYKNMK GGFIHVPYLP QQVLNKKNVP 

       190        200 
SMSLDNIVQA LVCSIKAILK EYNDE 

« Hide

References

[1]"The genome of Thermosipho africanus TCF52B: lateral genetic connections to the Firmicutes and Archaea."
Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D., Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.
J. Bacteriol. 191:1974-1978(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TCF52B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001185 Genomic DNA. Translation: ACJ76369.1.
RefSeqYP_002335710.1. NC_011653.1.

3D structure databases

ProteinModelPortalB7IEE2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING484019.THA_1947.

Protein family/group databases

MEROPSC15.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ76369; ACJ76369; THA_1947.
GeneID7071033.
KEGGtaf:THA_1947.
PATRIC23920964. VBITheAfr129358_1972.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2039.
HOGENOMHOG000242641.
KOK01304.
OMANDGENAY.
OrthoDBEOG6X1124.

Enzyme and pathway databases

BioCycTAFR484019:GJOH-1987-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_THEAB
AccessionPrimary (citable) accession number: B7IEE2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 36 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