ID   GPR_CLOP1               Reviewed;         325 AA.
AC   Q0TNR9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Germination protease;
DE            EC=3.4.24.78;
DE   AltName: Full=Spore protease;
DE   AltName: Full=GPR endopeptidase;
DE   AltName: Full=Germination proteinase;
DE   Flags: Precursor;
GN   Name=gpr; OrderedLocusNames=CPF_2298;
OS   Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA   DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA   Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA   Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA   Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA   Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA   Melville S.B., Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial
RT   pathogen, Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
CC   -!- FUNCTION: Initiates the rapid degradation of small, acid-soluble
CC       proteins during spore germination (By similarity).
CC   -!- CATALYTIC ACTIVITY: Endopeptidase action with P4 Glu or Asp, P1
CC       preferably Glu > Asp, P1' hydrophobic and P2' Ala.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- PTM: Autoproteolytically processed. The inactive tetrameric
CC       zymogen termed p46 autoprocesses to a smaller form termed p41,
CC       which is active only during spore germination (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase A25 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000246; ABG84499.1; -; Genomic_DNA.
DR   RefSeq; YP_696721.1; -.
DR   GeneID; 4201287; -.
DR   GenomeReviews; CP000246_GR; CPF_2298.
DR   KEGG; cpf:CPF_2298; -.
DR   TIGR; CPF_2298; -.
DR   HOGENOM; Q0TNR9; -.
DR   OMA; Q0TNR9; LMVTRHL.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:HAMAP.
DR   GO; GO:0009847; P:spore germination; IEA:HAMAP.
DR   HAMAP; MF_00626; -; 1.
DR   InterPro; IPR005080; Peptidase_A25.
DR   Gene3D; G3DSA:3.40.50.10100; Peptidase_A25; 1.
DR   Pfam; PF03418; Peptidase_A25; 1.
DR   PIRSF; PIRSF019549; Peptidase_A25; 1.
DR   ProDom; PD041835; Peptidase_A25; 1.
DR   TIGRFAMs; TIGR01441; GPR; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Protease; Zymogen.
FT   PROPEP        1      7       By similarity.
FT                                /FTId=PRO_0000316071.
FT   CHAIN         8    325       Germination protease.
FT                                /FTId=PRO_1000051610.
SQ   SEQUENCE   325 AA;  35548 MW;  9D8092C9C5A74F15 CRC64;
     MYNVRTDLAV ESREIYKHRY NREIDGVVFE EKTVEEDIKV TNVDILNEEG AKAMGKPIGR
     YVTIDIPEYT HYDGGIMDEV SHVVAASLEE LINLPEERTA LVVGLGNWNV TPDAIGPKVV
     GKLMVTRHLK KVMPDIIDDS VRPVCAIAPG VLGITGIETG EIIKSLVEKI NPDLVVCIDA
     LASRKLERVA RTIQISNTGI SPGAGVGNHR MQINEESLGI PVIALGVPTV VDAATIANDA
     MDLVLDEMIN QADAGKEFYN ILNNIDKNEK GMMIKSLLDP YVGDLMVTPK EIDDIIESVS
     KIIANGINIA LQPNMVLEDI NKFLN
//