PCP_STAAC
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 03-AUG-2022, entry version 104.
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}; OrderedLocusNames=SACOL2714;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; 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 EnsemblBacteria; AAW37362; AAW37362; SACOL2714.
DR KEGG; sac:SACOL2714; -.
DR HOGENOM; CLU_043960_4_0_9; -.
DR OMA; KLAYNHK; -.
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; -; 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 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