ID   PCP_STAAC               Reviewed;         212 AA.
AC   Q5HCK7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 110.
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=SACOL2714;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW37362.1; -; Genomic_DNA.
DR   RefSeq; WP_000547833.1; NC_002951.2.
DR   PDB; 3GIU; X-ray; 1.25 A; A/B=1-212.
DR   PDBsum; 3GIU; -.
DR   AlphaFoldDB; Q5HCK7; -.
DR   SMR; Q5HCK7; -.
DR   MEROPS; C15.001; -.
DR   KEGG; sac:SACOL2714; -.
DR   HOGENOM; CLU_043960_4_0_9; -.
DR   EvolutionaryTrace; Q5HCK7; -.
DR   Proteomes; UP000000530; Chromosome.
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; Peptidase C15, pyroglutamyl peptidase I-like; 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   NCBIfam; TIGR00504; pyro_pdase; 1.
DR   PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR   PANTHER; PTHR23402:SF1; RE07960P; 1.
DR   Pfam; PF01470; Peptidase_C15; 1.
DR   PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR   PRINTS; PR00706; PYROGLUPTASE.
DR   SUPFAM; SSF53182; Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase); 1.
DR   PROSITE; PS01334; PYRASE_CYS; 1.
DR   PROSITE; PS01333; PYRASE_GLU; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..212
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184731"
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"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   HELIX           18..25
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   STRAND          33..40
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   HELIX           44..57
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   HELIX           116..125
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   HELIX           140..154
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   STRAND          160..166
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:3GIU"
FT   HELIX           184..196
FT                   /evidence="ECO:0007829|PDB:3GIU"
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
//