GPR_GEOSW
ID GPR_GEOSW Reviewed; 372 AA.
AC C5D4U8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=GWCH70_2444;
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC unclassified Geobacillus.
OX NCBI_TaxID=471223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) 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; CP001638; ACS25140.1; -; Genomic_DNA.
DR RefSeq; WP_015864554.1; NC_012793.1.
DR AlphaFoldDB; C5D4U8; -.
DR SMR; C5D4U8; -.
DR STRING; 471223.GWCH70_2444; -.
DR MEROPS; A25.001; -.
DR EnsemblBacteria; ACS25140; ACS25140; GWCH70_2444.
DR KEGG; gwc:GWCH70_2444; -.
DR eggNOG; COG0680; Bacteria.
DR HOGENOM; CLU_055087_1_0_9; -.
DR OMA; PMGNYIT; -.
DR OrthoDB; 799376at2; -.
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_1000212308"
FT CHAIN 16..372
FT /note="Germination protease"
FT /id="PRO_1000212309"
SQ SEQUENCE 372 AA; 40941 MW; 86D6D00B91DD9F61 CRC64;
MNRSIDLSMY SVRTDLAIEA HEIAVEERLQ QKRESASPIE GVIIHDREID GIKLSHVEVT
EEGAKSIGKK PGNYLTIEAQ GIREHNTELQ QKVQDIFAKE FNAFLRKLDI RKESSCLVVG
LGNSNVTPDA LGPLTVENLL ITRHLFHLQP ESVEEGFRPV SAIAPGVMGT TGIETSDIIH
GIVEKTKPDF VIVIDALAAR SIERVNATIQ ISDTGIHPGS GVGNKRKELS KETLGIPVIS
IGVPTVVDAV SITSDTIDFI LKHFGREMRE GKRPSSALAP AGWTFGKKKR LTEEDMPSTE
QRSTFLGIIG TLEEEEKRRL IYEVLSPLGH NLMVTPKEVD MFIEDMANLL ASGLNAALHE
QIDQDNTGSY TH