ID   GPR_CLOPE               Reviewed;         325 AA.
AC   Q8XIS3;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Germination protease {ECO:0000255|HAMAP-Rule:MF_00626};
DE            EC=3.4.24.78 {ECO:0000255|HAMAP-Rule:MF_00626};
DE   AltName: Full=GPR endopeptidase {ECO:0000255|HAMAP-Rule:MF_00626};
DE   AltName: Full=Germination proteinase {ECO:0000255|HAMAP-Rule:MF_00626};
DE   AltName: Full=Spore protease {ECO:0000255|HAMAP-Rule:MF_00626};
DE   Flags: Precursor;
GN   Name=gpr {ECO:0000255|HAMAP-Rule:MF_00626}; OrderedLocusNames=CPE2041;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC   -!- FUNCTION: Initiates the rapid degradation of small, acid-soluble
CC       proteins during spore germination. {ECO:0000255|HAMAP-Rule:MF_00626}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endopeptidase action with P4 Glu or Asp, P1 preferably Glu >
CC         Asp, P1' hydrophobic and P2' Ala.; EC=3.4.24.78;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00626};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00626}.
CC   -!- PTM: Autoproteolytically processed. The inactive tetrameric zymogen
CC       termed p46 autoprocesses to a smaller form termed p41, which is active
CC       only during spore germination. {ECO:0000255|HAMAP-Rule:MF_00626}.
CC   -!- SIMILARITY: Belongs to the peptidase A25 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00626}.
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DR   EMBL; BA000016; BAB81747.1; -; Genomic_DNA.
DR   RefSeq; WP_011010731.1; NC_003366.1.
DR   AlphaFoldDB; Q8XIS3; -.
DR   SMR; Q8XIS3; -.
DR   STRING; 195102.gene:10491311; -.
DR   MEROPS; A25.001; -.
DR   EnsemblBacteria; BAB81747; BAB81747; BAB81747.
DR   KEGG; cpe:CPE2041; -.
DR   HOGENOM; CLU_055087_1_0_9; -.
DR   OMA; PMGNYIT; -.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   GO; GO:0009847; P:spore germination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1450; -; 1.
DR   HAMAP; MF_00626; Germination_prot; 1.
DR   InterPro; IPR023430; Pept_HybD-like_dom_sf.
DR   InterPro; IPR005080; Peptidase_A25.
DR   Pfam; PF03418; Peptidase_A25; 2.
DR   PIRSF; PIRSF019549; Peptidase_A25; 1.
DR   SUPFAM; SSF53163; SSF53163; 1.
DR   TIGRFAMs; TIGR01441; GPR; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Zymogen.
FT   PROPEP          1..7
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00626"
FT                   /id="PRO_0000026874"
FT   CHAIN           8..325
FT                   /note="Germination protease"
FT                   /id="PRO_0000026875"
SQ   SEQUENCE   325 AA;  35634 MW;  AFE7E17827871ABF CRC64;
     MYNVRTDLAV ESREIYKHRY NREIDGVVFE EKTVEEDIKV TNVDILNEEG AKAMEKPIGR
     YVTIDIPEYT HYDGGIMDEV SHVVAASLEE LINLPEERTA LVVGLGNWNV TPDAIGPKVV
     GKLMVTRHLK KVMPDIIDDS VRPVCAIAPG VLGITGIETG EIIKSLVEKI KPDLVVCIDA
     LASRKLERVA RTIQISNTGI SPGAGVGNHR MQINEESLGI PVIALGVPTV VDAATIANDA
     MDLVLDEMIN QADAGKEFYN ILNNIDKNEK GMMIKSLLDP YVGDLMVTPK EIDDIIESVS
     KIIANGINIA LQPNMVLEDI NKFLN