ID   PCP_BACAN               Reviewed;         215 AA.
AC   Q81NT5; Q6HX05;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 130.
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=BA_3090, GBAA_3090, BAS2875;
OS   Bacillus anthracis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
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; AE016879; AAP26903.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT55184.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT70140.1; -; Genomic_DNA.
DR   RefSeq; NP_845417.1; NC_003997.3.
DR   RefSeq; WP_000859733.1; NZ_WXXJ01000001.1.
DR   RefSeq; YP_029133.1; NC_005945.1.
DR   PDB; 3LAC; X-ray; 2.00 A; A/B=1-215.
DR   PDBsum; 3LAC; -.
DR   AlphaFoldDB; Q81NT5; -.
DR   SMR; Q81NT5; -.
DR   STRING; 261594.GBAA_3090; -.
DR   MEROPS; C15.001; -.
DR   DNASU; 1086349; -.
DR   GeneID; 45022894; -.
DR   KEGG; ban:BA_3090; -.
DR   KEGG; bar:GBAA_3090; -.
DR   KEGG; bat:BAS2875; -.
DR   PATRIC; fig|198094.11.peg.3072; -.
DR   eggNOG; COG2039; Bacteria.
DR   HOGENOM; CLU_043960_4_0_9; -.
DR   OMA; VCNHVFY; -.
DR   OrthoDB; 9779738at2; -.
DR   EvolutionaryTrace; Q81NT5; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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; Reference proteome;
KW   Thiol protease.
FT   CHAIN           1..215
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184707"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT   STRAND          2..9
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   HELIX           19..25
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   TURN            26..29
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   STRAND          35..42
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   HELIX           48..60
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   STRAND          75..80
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   STRAND          82..85
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   STRAND          110..113
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   HELIX           118..127
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   STRAND          132..136
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   HELIX           142..154
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   STRAND          160..168
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:3LAC"
FT   HELIX           186..200
FT                   /evidence="ECO:0007829|PDB:3LAC"
SQ   SEQUENCE   215 AA;  23513 MW;  352437CBE86717A6 CRC64;
     MKTVLLTGFD PFGGESINPA WEVAKSLHEK TIGEYKIISK QVPTVFHKSI SVLKEYIEEL
     APEFIICIGQ AGGRPDITIE RVAINIDDAR IADNEGNQPV DVPVVEEGPA AYWSTLPMKA
     IVKKLQEEGI PASVSQTAGT FVCNHLFYGL MHELEKHDTK MKGGFIHIPF LPEQASNYPG
     QPSMSLSTIR KGIELAVEVT TTVEVDIVEV GGTTH
//