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Q65FR5 (PCP_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:BLi03263, BL02514
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

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_1000050123

Sites

Active site811 By similarity
Active site1441 By similarity
Active site1681 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65FR5 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 32896056DF4FAA7A

FASTA21523,277
        10         20         30         40         50         60 
MGKKVLLTGF DPFGGETVNP SWEAVKRLNG EEAEGVSIAA EQIPTVFHHS AAVLKKAIEK 

        70         80         90        100        110        120 
HKPDVVICAG QAGGRAHITP ERIAINIDDA RIPDNEDREP IDEPIAADGP AAYWSALPIK 

       130        140        150        160        170        180 
LIVKELRKNG IPASVSNSAG TFVCNHLFYQ LMHRIDRTSA NIRGGFIHIP FLPEQTIDKP 

       190        200        210 
EPSLSLETIV EGLRIAAVIS ALHEKDIRET GGSIS 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU24736.1.
AE017333 Genomic DNA. Translation: AAU42099.1.
RefSeqYP_006714571.1. NC_006322.1.
YP_080374.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65FR5.
SMRQ65FR5. Positions 1-211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL02514.

Protein family/group databases

MEROPSC15.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU24736; AAU24736; BL02514.
AAU42099; AAU42099; BLi03263.
GeneID3027696.
3099266.
KEGGbld:BLi03263.
bli:BL02514.
PATRIC18952276. VBIBacLic203714_3315.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2039.
HOGENOMHOG000242641.
KOK01304.
OMAKPNTPSM.
OrthoDBEOG6X1124.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-3233-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_BACLD
AccessionPrimary (citable) accession number: Q65FR5
Secondary accession number(s): Q62R74
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 70 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