ID   GPR_BACAC               Reviewed;         368 AA.
AC   C3L5S4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=BAMEG_4583;
OS   Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=568206;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 684 / NRRL 3495;
RA   Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA   Sutton G., Sims D.;
RT   "Genome sequence of Bacillus anthracis str. CDC 684.";
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; CP001215; ACP13083.1; -; Genomic_DNA.
DR   RefSeq; WP_000662639.1; NC_012581.1.
DR   AlphaFoldDB; C3L5S4; -.
DR   SMR; C3L5S4; -.
DR   MEROPS; A25.001; -.
DR   GeneID; 45024198; -.
DR   KEGG; bah:BAMEG_4583; -.
DR   HOGENOM; CLU_055087_1_0_9; -.
DR   OMA; PMGNYIT; -.
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_1000147251"
FT   CHAIN           16..368
FT                   /note="Germination protease"
FT                   /id="PRO_1000147252"
SQ   SEQUENCE   368 AA;  40605 MW;  7FA028D9D5D24865 CRC64;
     MKEPLDLSKY SVRTDLAVEA HQMLQERQEE QQQGIQGVIV KEREEEGIII TKVTIDEVAS
     ESMGKKPGNY LTLEVQGIRQ QDTELQQKVE RIFAKEFSYF LEEVGVTKEA SCLIVGLGNW
     NVTPDALGPI VVENVLVTRH LFQLQPESVE EGFRPVSAIR PGVMGITGIE TSDVIYGIIE
     KTKPDFVIAI DALAARSIER VNSTIQISDT GIHPGSGVGN KRKELSKETL GIPVIAIGVP
     TVVDAVSITS DTIDFILKHF GREMKEGNKP SRSLLPAGFT FGEKKKLTEE DMPDEKSRNM
     FLGAVGTLED EEKRKLIYEV LSPLGHNLMV TPKEVDAFIE DMANVIASGL NAALHHQIDQ
     DNTGAYTH