ID   GPR_BACC4               Reviewed;         367 AA.
AC   B7HCU7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=BCB4264_A4440;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
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 B4264.";
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; CP001176; ACK60733.1; -; Genomic_DNA.
DR   RefSeq; WP_000662616.1; NC_011725.1.
DR   AlphaFoldDB; B7HCU7; -.
DR   SMR; B7HCU7; -.
DR   MEROPS; A25.001; -.
DR   EnsemblBacteria; ACK60733; ACK60733; BCB4264_A4440.
DR   KEGG; bcb:BCB4264_A4440; -.
DR   HOGENOM; CLU_055087_1_0_9; -.
DR   OMA; PMGNYIT; -.
DR   Proteomes; UP000007096; 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_1000130528"
FT   CHAIN           16..367
FT                   /note="Germination protease"
FT                   /id="PRO_1000130529"
SQ   SEQUENCE   367 AA;  40336 MW;  C2B84689414B0A43 CRC64;
     MKEPLDLSKY SIRTDLAVEA HQMLQESQEE QKGIQGVIVK EREEEGTIIT KVTIDEAASE
     AMGKKPGNYL TLEVQGIRQQ DTELQQKVER IFAKEFSCFL EEVGVTKEAS CLIVGLGNWN
     VTPDALGPIV VENVLVTRHL FQLQPESVEE GFRPVSAIRP GVMGITGIET SDVIYGIIEK
     TNPDFVIAID ALAARSIERV NSTIQISDTG IHPGSGVGNK RKELSKDTLG IPVIAIGVPT
     VVDAVSITSD TIDFILKHFG REMKEGNKPS RSLLPAGFSF GEKKKLTEED MPDEKSRNMF
     LGAVGTLEEE EKRRLIYEVL SPLGHNLMVT PKEVDTFIED MANVIASGLN AALHHQIDQD
     NTGAYTH