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PCP1_STRPN
ID   PCP1_STRPN              Reviewed;         214 AA.
AC   P65678; Q97RG1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Pyrrolidone-carboxylate peptidase 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE            EC=3.4.19.3 {ECO:0000255|HAMAP-Rule:MF_00417};
DE   AltName: Full=5-oxoprolyl-peptidase 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE   AltName: Full=Pyroglutamyl-peptidase I 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE            Short=PGP-I 1 {ECO:0000255|HAMAP-Rule:MF_00417};
DE            Short=Pyrase 1 {ECO:0000255|HAMAP-Rule:MF_00417};
GN   Name=pcp1 {ECO:0000255|HAMAP-Rule:MF_00417}; Synonyms=pcp;
GN   OrderedLocusNames=SP_0860;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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; AE005672; AAK74988.1; -; Genomic_DNA.
DR   PIR; C95099; C95099.
DR   RefSeq; WP_000699369.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; P65678; -.
DR   SMR; P65678; -.
DR   STRING; 170187.SP_0860; -.
DR   MEROPS; C15.001; -.
DR   EnsemblBacteria; AAK74988; AAK74988; SP_0860.
DR   GeneID; 60232522; -.
DR   GeneID; 66805994; -.
DR   KEGG; spn:SP_0860; -.
DR   eggNOG; COG2039; Bacteria.
DR   OMA; KLAYNHK; -.
DR   PhylomeDB; P65678; -.
DR   BioCyc; SPNE170187:G1FZB-878-MON; -.
DR   Proteomes; UP000000585; 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   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..214
FT                   /note="Pyrrolidone-carboxylate peptidase 1"
FT                   /id="PRO_0000184739"
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   214 AA;  23420 MW;  A13FD934C3766BD0 CRC64;
     MKILVTGFNP FGGEKINPAL EAVKLLPSEI NGAEVRWVEI PTVFYKSSEV LEAEILRYQP
     DAVLCIGQAG GRTGLTPERV AINQDDARIP DNEGNQPIDT PIRIDGASAY FSSLPIKAMV
     QAIKKQGLPA VVSNSAGTFV CNHLMYQALY LVDKKFPNMR AGFMHIPYMM EQVVNKPNTA
     GMSLCDIVRG IEVAIEAIVD YKDKDLQLVG GETH
 
 
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