GPR_OCEIH
ID GPR_OCEIH Reviewed; 367 AA.
AC Q8CXC9;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=OB1975;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13931.1; -; Genomic_DNA.
DR RefSeq; WP_011066372.1; NC_004193.1.
DR AlphaFoldDB; Q8CXC9; -.
DR SMR; Q8CXC9; -.
DR STRING; 221109.22777659; -.
DR MEROPS; A25.001; -.
DR PRIDE; Q8CXC9; -.
DR EnsemblBacteria; BAC13931; BAC13931; BAC13931.
DR KEGG; oih:OB1975; -.
DR eggNOG; COG0680; Bacteria.
DR HOGENOM; CLU_055087_1_0_9; -.
DR OMA; PMGNYIT; -.
DR OrthoDB; 799376at2; -.
DR PhylomeDB; Q8CXC9; -.
DR Proteomes; UP000000822; 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; Reference proteome; Zymogen.
FT PROPEP 1..13
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00626"
FT /id="PRO_0000026878"
FT CHAIN 14..367
FT /note="Germination protease"
FT /id="PRO_0000026879"
FT REGION 267..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 40467 MW; 3F4985F73F2CE5C7 CRC64;
MEEQQIPFQV RTDLAIEAKD MYTESKPEET NDKEIKGVTF KERSVKDIKV SYVDIDEEGE
KLLGKKPGSY VTIYADGVKK QDTDRQGQAA QVLAKELEDL MRKNNVTKES TCLVVGLGNW
NVTPDALGPM TVEKVLVTSH LFRLQYETVA QGYRDVAAVT PGVMGVTGIE TSDIIFGIVE
KYKPDLVIAV DALASRSINR VNETIQLSDT GIHPGSGVGN KRKEISKKTL GIPVIAIGVP
TVVDAVTITS DTIDYVLKHF GREWKEKDDP SKSLTPAGMS FGNRKLTDED LPNMEKRKTV
LGIVGELSDE EKRKLITEVL TPLGHNLMVT PKEVDGFMID MAEVLANGIN AALHEKVDVD
NFANYSR
