GPR_BACVZ
ID GPR_BACVZ Reviewed; 368 AA.
AC A7Z6W8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=RBAM_023840;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS74744.1; -; Genomic_DNA.
DR RefSeq; WP_007408268.1; NC_009725.2.
DR AlphaFoldDB; A7Z6W8; -.
DR SMR; A7Z6W8; -.
DR STRING; 326423.RBAM_023840; -.
DR MEROPS; A25.001; -.
DR EnsemblBacteria; ABS74744; ABS74744; RBAM_023840.
DR KEGG; bay:RBAM_023840; -.
DR HOGENOM; CLU_055087_1_0_9; -.
DR OMA; PMGNYIT; -.
DR Proteomes; UP000001120; 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; -; 2.
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..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00626"
FT /id="PRO_0000316069"
FT CHAIN 17..368
FT /note="Germination protease"
FT /id="PRO_1000051608"
SQ SEQUENCE 368 AA; 40191 MW; 68F281B7C602B00A CRC64;
MKNNELDVNQ FLIRTDLAVE TKQAVKDGQA GQKKEINGFI EKERDKGGIK VRTVDITKEG
AELSGKKQGR YVTIEAQGVR EHDSDMQEKV TEVFAEEFSA YLSALKIPKD ASCLIVGLGN
WNVTPDALGP LVTENLLVTR HLFRLQPENV QEGYRPVSAL APGVMGLTGI ETSDIIQGVI
KESKPDFVIA VDALAARAVE RVNTTIQFSD TGIHPGSGVG NKRKELSKET LGIPVIAIGV
PTVVDAVTIA SDTVDYILKH FGREMKDDSP SRSLVPAGMN FGKKKVLTDE DLPGEKERQS
FLGIVGTLDE NEKRQLIHEV LSPLGHNLMV TPKEIDTFID DMANVLANGL NTALHEKVSQ
DNKGSYNH