ID   GPR_BACC2               Reviewed;         367 AA.
AC   B7IYH4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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};
GN   OrderedLocusNames=BCG9842_B0796;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001186; ACK94068.1; -; Genomic_DNA.
DR   RefSeq; WP_000662644.1; NC_011772.1.
DR   AlphaFoldDB; B7IYH4; -.
DR   SMR; B7IYH4; -.
DR   MEROPS; A25.001; -.
DR   EnsemblBacteria; ACK94068; ACK94068; BCG9842_B0796.
DR   KEGG; bcg:BCG9842_B0796; -.
DR   HOGENOM; CLU_055087_1_0_9; -.
DR   OMA; PMGNYIT; -.
DR   Proteomes; UP000006744; 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; 1.
DR   PIRSF; PIRSF019549; Peptidase_A25; 1.
DR   SUPFAM; SSF53163; SSF53163; 1.
DR   TIGRFAMs; TIGR01441; GPR; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Zymogen.
FT   PROPEP          1..15
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00626"
FT                   /id="PRO_1000130526"
FT   CHAIN           16..367
FT                   /note="Germination protease"
FT                   /id="PRO_1000130527"
SQ   SEQUENCE   367 AA;  40396 MW;  25715C5CBACAA930 CRC64;
     MKEPLDLSKY SVRTDLAVEA HQMLQESQEE QKGIQGVIVK EREEEGTIIT KVTIDEAASE
     AMGKKPGNYL TLEVQGIRQQ DTELQQKVER IFAKEFSYFL EEVGVTKEAS CLIVGLGNWN
     VTPDALGPIV VENVLVTRHL FQLQPESVEE GFRPVSAIRP GVMGITGIET SDVIYGIIEK
     TNPDFVIAID ALAARSIERV NSTIQISDTG IHPGSGVGNK RKELSKETLG IPVIAIGVPT
     VVDAVSITSD TIDFILKHFG REMKEGNKPS RSLLPAGFSF GEKKKLTEED MPDEKSRNMF
     LGAVGTLEEE EKRRLIYEVL SPLGHNLMVT PKEVDTFIED MANVIASGLN AALHHQIDQD
     NTGAYTH