ID   GPR_BACCQ               Reviewed;         367 AA.
AC   B9IY88;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-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}; OrderedLocusNames=BCQ_4107;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM14534.1; -; Genomic_DNA.
DR   RefSeq; WP_000662638.1; NC_011969.1.
DR   AlphaFoldDB; B9IY88; -.
DR   SMR; B9IY88; -.
DR   MEROPS; A25.001; -.
DR   EnsemblBacteria; ACM14534; ACM14534; BCQ_4107.
DR   GeneID; 64199666; -.
DR   KEGG; bcq:BCQ_4107; -.
DR   HOGENOM; CLU_055087_1_0_9; -.
DR   OMA; PMGNYIT; -.
DR   Proteomes; UP000000441; 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_1000147255"
FT   CHAIN           16..367
FT                   /note="Germination protease"
FT                   /id="PRO_1000147256"
SQ   SEQUENCE   367 AA;  40451 MW;  B91C82F3FB73B211 CRC64;
     MKEPLDLSKY SVRTDLAVEA HQMLQERQEE QQGIQGVVVK EREEEGITIT KVTIDEVASE
     SMGKKPGNYL TLEVQGIRQQ DTELQQKVER IFAKEFSYFL EEVGVTKEAS CLIVGLGNWN
     VTPDALGPIV VENVLVTRHL FQLQPESVEE GFRPVSAIRP GVMGITGIET SDVIYGIIEK
     TKPDFVIAID ALAARSIERV NSTIQISDTG IHPGSGVGNK RKELSKETLG IPVIAIGVPT
     VVDAVSITSD TIDFILKHFG REMKEGNKPS RSLLPAGFTF GEKKKLTEED MPDEKSRNMF
     LGAVGTLEDE EKRKLIYEVL SPLGHNLMVT PKEVDAFIED MANVIASGLN AALHHQIDQD
     NTGAYTH