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Q5HCK7 (PCP_STAAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:SACOL2714
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete 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 – 212212Pyrrolidone-carboxylate peptidase HAMAP-Rule MF_00417
PRO_0000184731

Sites

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

Secondary structure

............................... 212
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5HCK7 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: BBC76CD8FC43ACBC

FASTA21223,167
        10         20         30         40         50         60 
MHILVTGFAP FDNQNINPSW EAVTQLEDII GTHTIDKLKL PTSFKKVDNI INKTLASNHY 

        70         80         90        100        110        120 
DVVLAIGQAG GRNAITPERV AINIDDARIP DNDDFQPIDQ AIHLDGAPAY FSNLPVKAMT 

       130        140        150        160        170        180 
QSIINQGLPG ALSNSAGTFV CNHTLYHLGY LQDKHYPHLR FGFIHVPYIP EQVIGKPDTP 

       190        200        210 
SMPLEKIVAG LTAAIEAISN DEDLHLALGT TE 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: COL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000046 Genomic DNA. Translation: AAW37362.1.
RefSeqYP_187500.1. NC_002951.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GIUX-ray1.25A/B1-212[»]
ProteinModelPortalQ5HCK7.
SMRQ5HCK7. Positions 1-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93062.SACOL2714.

Protein family/group databases

MEROPSC15.001.

Proteomic databases

PRIDEQ5HCK7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW37362; AAW37362; SACOL2714.
GeneID3238254.
KEGGsac:SACOL2714.
PATRIC19531676. VBIStaAur112458_2639.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2039.
HOGENOMHOG000242641.
KOK01304.
OMAKPNTPSM.
OrthoDBEOG6X1124.

Enzyme and pathway databases

BioCycSAUR93062:GCEP-2696-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...

Other

EvolutionaryTraceQ5HCK7.

Entry information

Entry namePCP_STAAC
AccessionPrimary (citable) accession number: Q5HCK7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 66 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references