ID   GPR_BACCN               Reviewed;         367 AA.
AC   A7GT16;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Bcer98_3048;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS23274.1; -; Genomic_DNA.
DR   RefSeq; WP_012095512.1; NC_009674.1.
DR   AlphaFoldDB; A7GT16; -.
DR   SMR; A7GT16; -.
DR   STRING; 315749.Bcer98_3048; -.
DR   MEROPS; A25.001; -.
DR   EnsemblBacteria; ABS23274; ABS23274; Bcer98_3048.
DR   GeneID; 56418593; -.
DR   KEGG; bcy:Bcer98_3048; -.
DR   eggNOG; COG0680; Bacteria.
DR   HOGENOM; CLU_055087_1_0_9; -.
DR   OMA; PMGNYIT; -.
DR   OrthoDB; 799376at2; -.
DR   Proteomes; UP000002300; 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_1000082606"
FT   CHAIN           16..367
FT                   /note="Germination protease"
FT                   /id="PRO_1000082607"
SQ   SEQUENCE   367 AA;  40453 MW;  FA591DA4521B6475 CRC64;
     MKEPLDLSKY AVRTDLAVEA HQMLQERQQE NTGIQGVIIK EREEEGMTIT KVTIDESASE
     AMGKKAGNYL TLEVQGIRQQ DTELQRKVER IFAKEFAYFL EEIGVKKEAS CLIVGLGNWN
     VTPDALGPIV VENVLVTRHL FKLQPESVED GYRPVSAIRP GVMGITGIET SDVIFGIIEK
     TKPDFVIAID ALAARSIERV NSTIQISDTG IHPGSGVGNK RKELSQETLG IPVIAIGVPT
     VVDAVSITSD TIDFILKHFG REMKEGDKPS RSLLPAGFTF GEKKKLTEED MPDEKSRNMF
     LGAVGMLEEE EKRKLIYEVL APLGHNLMVT PKEVDAFIED MANVIASGLN AALHHQIDQD
     NTGAYTH