PCP_STAAT
ID PCP_STAAT Reviewed; 212 AA.
AC A8Z5J1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Pyrrolidone-carboxylate peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE EC=3.4.19.3 {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=5-oxoprolyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=Pyroglutamyl-peptidase I {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=PGP-I {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=Pyrase {ECO:0000255|HAMAP-Rule:MF_00417};
GN Name=pcp {ECO:0000255|HAMAP-Rule:MF_00417};
GN OrderedLocusNames=USA300HOU_2692;
OS Staphylococcus aureus (strain USA300 / TCH1516).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=451516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300 / TCH1516;
RX PubMed=17986343; DOI=10.1186/1471-2180-7-99;
RA Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S.,
RA Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O.,
RA Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M.,
RA Hemphill L., Ding Y., Dugan S., Blyth P.R., Buhay C.J., Dinh H.H.,
RA Hawes A.C., Holder M., Kovar C.L., Lee S.L., Liu W., Nazareth L.V.,
RA Wang Q., Zhou J., Kaplan S.L., Weinstock G.M.;
RT "Subtle genetic changes enhance virulence of methicillin resistant and
RT sensitive Staphylococcus aureus.";
RL BMC Microbiol. 7:99-99(2007).
CC -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC residues except L-proline. {ECO:0000255|HAMAP-Rule:MF_00417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal pyroglutamyl group from a
CC polypeptide, the second amino acid generally not being Pro.;
CC EC=3.4.19.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00417};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00417}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00417}.
CC -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000255|HAMAP-
CC Rule:MF_00417}.
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DR EMBL; CP000730; ABX30678.1; -; Genomic_DNA.
DR RefSeq; WP_000547833.1; NC_010079.1.
DR AlphaFoldDB; A8Z5J1; -.
DR SMR; A8Z5J1; -.
DR MEROPS; C15.001; -.
DR KEGG; sax:USA300HOU_2692; -.
DR HOGENOM; CLU_043960_4_0_9; -.
DR OMA; KLAYNHK; -.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00501; Peptidase_C15; 1.
DR Gene3D; 3.40.630.20; -; 1.
DR HAMAP; MF_00417; Pyrrolid_peptidase; 1.
DR InterPro; IPR000816; Peptidase_C15.
DR InterPro; IPR016125; Peptidase_C15-like.
DR InterPro; IPR036440; Peptidase_C15-like_sf.
DR InterPro; IPR029762; PGP-I_bact-type.
DR InterPro; IPR033694; PGPEP1_Cys_AS.
DR InterPro; IPR033693; PGPEP1_Glu_AS.
DR PANTHER; PTHR23402; PTHR23402; 1.
DR Pfam; PF01470; Peptidase_C15; 1.
DR PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR PRINTS; PR00706; PYROGLUPTASE.
DR SUPFAM; SSF53182; SSF53182; 1.
DR TIGRFAMs; TIGR00504; pyro_pdase; 1.
DR PROSITE; PS01334; PYRASE_CYS; 1.
DR PROSITE; PS01333; PYRASE_GLU; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Thiol protease.
FT CHAIN 1..212
FT /note="Pyrrolidone-carboxylate peptidase"
FT /id="PRO_1000080517"
FT ACT_SITE 78
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT ACT_SITE 141
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
SQ SEQUENCE 212 AA; 23167 MW; BBC76CD8FC43ACBC CRC64;
MHILVTGFAP FDNQNINPSW EAVTQLEDII GTHTIDKLKL PTSFKKVDNI INKTLASNHY
DVVLAIGQAG GRNAITPERV AINIDDARIP DNDDFQPIDQ AIHLDGAPAY FSNLPVKAMT
QSIINQGLPG ALSNSAGTFV CNHTLYHLGY LQDKHYPHLR FGFIHVPYIP EQVIGKPDTP
SMPLEKIVAG LTAAIEAISN DEDLHLALGT TE