PCP2_STRPN
ID PCP2_STRPN Reviewed; 214 AA.
AC Q97NG9;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Pyrrolidone-carboxylate peptidase 2 {ECO:0000255|HAMAP-Rule:MF_00417};
DE EC=3.4.19.3 {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=5-oxoprolyl-peptidase 2 {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=Pyroglutamyl-peptidase I 2 {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=PGP-I 2 {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=Pyrase 2 {ECO:0000255|HAMAP-Rule:MF_00417};
GN Name=pcp2 {ECO:0000255|HAMAP-Rule:MF_00417}; OrderedLocusNames=SP_2060;
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; AAK76124.1; -; Genomic_DNA.
DR PIR; C95241; C95241.
DR RefSeq; WP_000866913.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97NG9; -.
DR SMR; Q97NG9; -.
DR STRING; 170187.SP_2060; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; AAK76124; AAK76124; SP_2060.
DR KEGG; spn:SP_2060; -.
DR eggNOG; COG2039; Bacteria.
DR OMA; HHIATRA; -.
DR PhylomeDB; Q97NG9; -.
DR BioCyc; SPNE170187:G1FZB-2129-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 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.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Thiol protease.
FT CHAIN 1..214
FT /note="Pyrrolidone-carboxylate peptidase 2"
FT /id="PRO_0000184741"
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; 23406 MW; 17B0A1C4F4D1A7F8 CRC64;
MKVLVTGFEP FGGEKGNPAL EAIKGLPAEI HGAEVRWLEV PTVFHKSAQV LEEEMNRYQP
DFVLCIGQAG GRTSLTPERV TINQDDACIS DNEDNQPIDR PIRPDGASAY FSSLPIKAMV
QAIKKEGLPA SVSNTAGTFV CSHLMYQALY LVEKKSPYVK AGFMHIPYMM EQVVNRPTTP
AMSLVDIRRG IEAAIGAIIE HGDQELKLVG GETH