GPR_ALKHC
ID GPR_ALKHC Reviewed; 372 AA.
AC Q9KD78;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=BH1340;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05059.1; -; Genomic_DNA.
DR PIR; D83817; D83817.
DR RefSeq; WP_010897506.1; NC_002570.2.
DR AlphaFoldDB; Q9KD78; -.
DR SMR; Q9KD78; -.
DR STRING; 272558.10173956; -.
DR MEROPS; A25.001; -.
DR EnsemblBacteria; BAB05059; BAB05059; BAB05059.
DR KEGG; bha:BH1340; -.
DR eggNOG; COG0680; Bacteria.
DR HOGENOM; CLU_055087_1_0_9; -.
DR OMA; PMGNYIT; -.
DR OrthoDB; 799376at2; -.
DR Proteomes; UP000001258; 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..15
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00626"
FT /id="PRO_0000026862"
FT CHAIN 16..372
FT /note="Germination protease"
FT /id="PRO_0000026863"
SQ SEQUENCE 372 AA; 40627 MW; 480F6DDE0D583661 CRC64;
MVKELNLEQY NVRTDLAIEA HDIVKEQEAQ EAKQPASTVE GFDIEETVMD GVKVSKVVIH
PLGAERTGKK AGRYLTFESQ GIRKKDTDIQ EKMERVFAQQ FSQFMGELGI TKDHTCLVVG
LGNWNVTPDA LGPITVENLL VTRHLFTLAP EEVGEGFRPV SAIAPGVMGV TGIETSDVIY
GIIEQTKPDF VIAVDALASR SIERVNATIQ VSDTGIHPGS GVGNKRKELS KETLGIPVIA
VGIPTVVDAV TITSDAIDYV LKHFGRELRE REKPSRALAP AGMTFGERRE LTDEDLPPEE
KRKTFLGMMG TLPEGEKRQL IQEVLAPLGH NLMVTPKEVD VFIEDMANVI ASGLNAALHQ
GVNQDNVGAY TH
