ID   GPR_BACMK               Reviewed;         367 AA.
AC   A9VHU8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=BcerKBAB4_4172;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
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; CP000903; ABY45333.1; -; Genomic_DNA.
DR   RefSeq; WP_002088693.1; NC_010184.1.
DR   AlphaFoldDB; A9VHU8; -.
DR   SMR; A9VHU8; -.
DR   STRING; 315730.BcerKBAB4_4172; -.
DR   MEROPS; A25.001; -.
DR   EnsemblBacteria; ABY45333; ABY45333; BcerKBAB4_4172.
DR   GeneID; 66266104; -.
DR   KEGG; bwe:BcerKBAB4_4172; -.
DR   eggNOG; COG0680; Bacteria.
DR   HOGENOM; CLU_055087_1_0_9; -.
DR   OMA; PMGNYIT; -.
DR   Proteomes; UP000002154; 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_1000130532"
FT   CHAIN           16..367
FT                   /note="Germination protease"
FT                   /id="PRO_1000130533"
SQ   SEQUENCE   367 AA;  40434 MW;  7EAFD264EB0A3718 CRC64;
     MKEPLDLSKY SVRTDLAVEA HQMLQERQEE QKGIQGVIVK EREEEGVTIT KVTIDEIASE
     SMGKKPGSYL TLEVQGIRQQ DTELQQKVER IFAKEFSYFL EEVGVSKEAS CLIVGLGNWN
     VTPDALGPIV VENVLVTRHL FKLQPESVEE GFRPVSAIRP GVMGITGIET SDVIYGIIEK
     TKPDFVIAID ALAARSIERV NSTIQISDTG IHPGSGVGNK RKELSKETLG IPVIAIGVPT
     VVDAVSITSD TIDFILKHFG RELKEGNKPS RSLLPAGFTF GEKKKLTEED MPDEKSRNMF
     LGAIGTLEEE EKRKLIYEVL SPLGHNLMVT PKEVDAFIED MANVIASGLN AALHHQIDQD
     NTGAYTH