(data stored in ACNUC7421 zone)

SWISSPROT: PCP_BACSU

ID   PCP_BACSU               Reviewed;         215 AA.
AC   P28618;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   11-DEC-2019, entry version 133.
DE   RecName: Full=Pyrrolidone-carboxylate peptidase;
DE            EC=3.4.19.3;
DE   AltName: Full=5-oxoprolyl-peptidase;
DE   AltName: Full=Pyroglutamyl-peptidase I;
DE            Short=PGP-I;
DE            Short=Pyrase;
GN   Name=pcp; OrderedLocusNames=BSU02650;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=1353026; DOI=10.1016/0014-5793(92)80656-2;
RA   Awade A., Cleuziat P., Gonzales T., Robert-Baudouy J.;
RT   "Characterization of the pcp gene encoding the pyrrolidone carboxyl
RT   peptidase of Bacillus subtilis.";
RL   FEBS Lett. 305:67-73(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7704254; DOI=10.1099/13500872-141-2-269;
RA   Ogawa K., Akagawa E., Nakamura K., Yamane K.;
RT   "Determination of a 21548 bp nucleotide sequence around the 24 degrees
RT   region of the Bacillus subtilis chromosome.";
RL   Microbiology 141:269-275(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-18, AND CHARACTERIZATION.
RX   PubMed=1362573; DOI=10.1016/0378-4347(92)80014-h;
RA   Gonzales T., Awade A., Besson C., Robert-Baudouy J.;
RT   "Purification and characterization of recombinant pyrrolidone carboxyl
RT   peptidase of Bacillus subtilis.";
RL   J. Chromatogr. A 584:101-107(1992).
CC   -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC       residues except L-proline.
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;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000305}.
DR   EMBL; X66034; CAA46833.1; -; Genomic_DNA.
DR   EMBL; D30808; BAA06485.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12059.1; -; Genomic_DNA.
DR   PIR; S23432; S23432.
DR   RefSeq; NP_388147.1; NC_000964.3.
DR   RefSeq; WP_003246307.1; NZ_JNCM01000030.1.
DR   SMR; P28618; -.
DR   STRING; 224308.BSU02650; -.
DR   MEROPS; C15.001; -.
DR   PaxDb; P28618; -.
DR   PRIDE; P28618; -.
DR   EnsemblBacteria; CAB12059; CAB12059; BSU02650.
DR   GeneID; 938396; -.
DR   KEGG; bsu:BSU02650; -.
DR   PATRIC; fig|224308.179.peg.275; -.
DR   eggNOG; ENOG4108KN7; Bacteria.
DR   eggNOG; COG2039; LUCA.
DR   HOGENOM; HOG000242641; -.
DR   InParanoid; P28618; -.
DR   KO; K01304; -.
DR   OMA; LCGYIYL; -.
DR   PhylomeDB; P28618; -.
DR   BioCyc; BSUB:BSU02650-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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;
DR   PRODOM; P28618.
DR   SWISS-2DPAGE; P28618.
KW   Cytoplasm; Direct protein sequencing; Hydrolase; Protease;
KW   Reference proteome; Thiol protease.
FT   CHAIN           1..215
FT                   /note="Pyrrolidone-carboxylate peptidase"
FT                   /id="PRO_0000184713"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  23774 MW;  A88041177BCCFE24 CRC64;
     MRKKVLITGF DPFDKETVNP SWEAAKRLNG FETEEAIITA EQIPTVFRSA LDTLRQAIQK
     HQPDIVICVG QAGGRMQITP ERVAINLADA RIPDNEGHQP IDEEISPDGP AAYWTRLPVK
     RMTAKMKEHG IPAAVSYTAG TFVCNYLFYG LMDHISRTSP HIRGGFIHIP YIPQQTIDKT
     APSLSLDTIV RALRIAAVTA AQYDEDVKSP GGTLH
//

If you have problems or comments...

PBIL Back to PBIL home page