Q5HCK7 (PCP_STAAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	pcp
Ordered Locus Names:	SACOL2714

Organism

Staphylococcus aureus (strain COL) [Complete proteome] [HAMAP]

Taxonomic identifier

93062 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	212 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Molecular function	Hydrolase Protease Thiol protease
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW pyroglutamyl-peptidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 212

212

Pyrrolidone-carboxylate peptidase HAMAP-Rule MF_00417

PRO_0000184731

Sites

Active site

78

1

By similarity

Active site

141

1

By similarity

Active site

165

1

By similarity

Secondary structure

1

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212

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Helix

18 – 25

8

Beta strand

28 – 30

3

Beta strand

33 – 40

8

Helix

44 – 57

14

Beta strand

61 – 68

8

Beta strand

74 – 78

5

Beta strand

80 – 83

4

Beta strand

98 – 100

3

Beta strand

108 – 111

4

Helix

116 – 125

10

Helix

140 – 154

15

Beta strand

160 – 166

7

Helix

170 – 173

4

Helix

184 – 196

13

Sequences

	Sequence		Length	Mass (Da)
	Q5HCK7 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: BBC76CD8FC43ACBC	FASTA	212	23,167
	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

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. , 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.

RefSeq

YP_187500.1. NC_002951.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GIU	X-ray	1.25	A/B	1-212	[»]

ProteinModelPortal

Q5HCK7.

SMR

Q5HCK7. Positions 1-212.

ModBase

Search...

Protein-protein interaction databases

STRING

93062.SACOL2714.

Protein family/group databases

MEROPS

C15.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAW37362; AAW37362; SACOL2714.

GeneID

3238254.

KEGG

sac:SACOL2714.

PATRIC

19531676. VBIStaAur112458_2639.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG2039.

HOGENOM

HOG000242641.

KO

K01304.

OMA

AYFTQLP.

ProtClustDB

PRK13197.

Enzyme and pathway databases

BioCyc

SAUR93062:GCEP-2696-MONOMER.

Family and domain databases

Gene3D

3.40.630.20. 1 hit.

HAMAP

MF_00417. Pyrrolid_peptidase.

InterPro

IPR000816. Peptidase_C15.
IPR016125. Peptidase_C15-like.
[Graphical view]

PANTHER

PTHR23402. PTHR23402. 1 hit.

Pfam

PF01470. Peptidase_C15. 1 hit.
[Graphical view]

PIRSF

PIRSF015592. Prld-crbxl_pptds. 1 hit.

PRINTS

PR00706. PYROGLUPTASE.

SUPFAM

SSF53182. Peptidase_C15-like. 1 hit.

TIGRFAMs

TIGR00504. pyro_pdase. 1 hit.

PROSITE

PS01334. PYRASE_CYS. 1 hit.
PS01333. PYRASE_GLU. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5HCK7.

Entry information

Entry name

PCP_STAAC

Accession

Primary (citable) accession number: Q5HCK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	February 15, 2005
Last modified:	May 29, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program