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Protein

Pyrrolidone-carboxylate peptidase

Gene

pcp

Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

pH dependencei

Optimum pH is 6.5. Stable from pH 7.0 to 9.0.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei81 – 811
Active sitei144 – 1441
Active sitei168 – 1681

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Protein family/group databases

MEROPSiC15.001.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:pcp
OrganismiBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifieri1390 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681C → S: No loss of activity. 1 Publication
Mutagenesisi144 – 1441C → S: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Pyrrolidone-carboxylate peptidasePRO_0000184706Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi326423.RBAM_002960.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Helixi20 – 278Combined sources
Turni28 – 303Combined sources
Beta strandi36 – 438Combined sources
Helixi49 – 6113Combined sources
Beta strandi64 – 718Combined sources
Beta strandi77 – 8610Combined sources
Beta strandi111 – 1144Combined sources
Helixi119 – 12810Combined sources
Helixi143 – 15816Combined sources
Beta strandi163 – 1697Combined sources
Helixi173 – 1753Combined sources
Beta strandi177 – 1793Combined sources
Helixi186 – 20217Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AUGX-ray2.00A/B/C/D1-215[»]
3RNZX-ray2.01A/B/C/D1-215[»]
3RO0X-ray1.50A/B/C/D1-215[»]
ProteinModelPortaliP46107.
SMRiP46107. Positions 1-210.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46107.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C15 family.Curated

Phylogenomic databases

eggNOGiENOG4108KN7. Bacteria.
COG2039. LUCA.

Family and domain databases

Gene3Di3.40.630.20. 1 hit.
HAMAPiMF_00417. Pyrrolid_peptidase.
InterProiIPR000816. Peptidase_C15.
IPR016125. Peptidase_C15-like.
IPR029762. PGP-I_bact-type.
[Graphical view]
PANTHERiPTHR23402. PTHR23402. 1 hit.
PfamiPF01470. Peptidase_C15. 1 hit.
[Graphical view]
PIRSFiPIRSF015592. Prld-crbxl_pptds. 1 hit.
PRINTSiPR00706. PYROGLUPTASE.
TIGRFAMsiTIGR00504. pyro_pdase. 1 hit.
PROSITEiPS01334. PYRASE_CYS. 1 hit.
PS01333. PYRASE_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKKVLLTGF DPFGGETVNP SWEAVKRLNG AAEGPASIVS EQVPTVFYKS
60 70 80 90 100
LAVLREAIKK HQPDIIICVG QAGGRMQITP ERVAINLNEA RIPDNEGNQP
110 120 130 140 150
VGEDISQGGP AAYWTGLPIK RIVEEIKKEG IPAAVSYTAG TFVCNHLFYG
160 170 180 190 200
LMDEISRHHP HIRGGFIHIP YIPEQTLQKS APSLSLDHIT KALKIAAVTA
210
AVHEDDIETG GGELH
Length:215
Mass (Da):23,287
Last modified:November 1, 1995 - v1
Checksum:i731A9F80733E807C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11035 Genomic DNA. Translation: BAA01791.1.
PIRiJX0244.
RefSeqiWP_013350909.1. NZ_LQYP01000011.1.

Genome annotation databases

GeneIDi9780258.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11035 Genomic DNA. Translation: BAA01791.1.
PIRiJX0244.
RefSeqiWP_013350909.1. NZ_LQYP01000011.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AUGX-ray2.00A/B/C/D1-215[»]
3RNZX-ray2.01A/B/C/D1-215[»]
3RO0X-ray1.50A/B/C/D1-215[»]
ProteinModelPortaliP46107.
SMRiP46107. Positions 1-210.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi326423.RBAM_002960.

Protein family/group databases

MEROPSiC15.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9780258.

Phylogenomic databases

eggNOGiENOG4108KN7. Bacteria.
COG2039. LUCA.

Miscellaneous databases

EvolutionaryTraceiP46107.

Family and domain databases

Gene3Di3.40.630.20. 1 hit.
HAMAPiMF_00417. Pyrrolid_peptidase.
InterProiIPR000816. Peptidase_C15.
IPR016125. Peptidase_C15-like.
IPR029762. PGP-I_bact-type.
[Graphical view]
PANTHERiPTHR23402. PTHR23402. 1 hit.
PfamiPF01470. Peptidase_C15. 1 hit.
[Graphical view]
PIRSFiPIRSF015592. Prld-crbxl_pptds. 1 hit.
PRINTSiPR00706. PYROGLUPTASE.
TIGRFAMsiTIGR00504. pyro_pdase. 1 hit.
PROSITEiPS01334. PYRASE_CYS. 1 hit.
PS01333. PYRASE_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Pyroglutamyl peptidase gene from Bacillus amyloliquefaciens: cloning, sequencing, expression, and crystallization of the expressed enzyme."
    Yoshimoto T., Shimoda T., Kitazono A., Kabashima T., Ito K., Tsuru D.
    J. Biochem. 113:67-73(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF CYS-68 AND CYS-144.
  2. "The crystal structure of pyroglutamyl peptidase I from Bacillus amyloliquefaciens reveals a new structure for a cysteine protease."
    Odagaki Y., Hayashi A., Okada K., Hirotsu K., Kabashima T., Ito K., Yoshimoto T., Tsuru D., Sato M., Clardy J.
    Structure 7:399-411(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiPCP_BACAM
AccessioniPrimary (citable) accession number: P46107
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.