ID   GPR_CLOTE               Reviewed;         323 AA.
AC   P59406;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=CTC_02040;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO36542.1; -; Genomic_DNA.
DR   RefSeq; WP_011100200.1; NC_004557.1.
DR   AlphaFoldDB; P59406; -.
DR   SMR; P59406; -.
DR   STRING; 212717.CTC_02040; -.
DR   MEROPS; A25.001; -.
DR   EnsemblBacteria; AAO36542; AAO36542; CTC_02040.
DR   GeneID; 64179850; -.
DR   KEGG; ctc:CTC_02040; -.
DR   HOGENOM; CLU_055087_1_0_9; -.
DR   OMA; PMGNYIT; -.
DR   OrthoDB; 799376at2; -.
DR   Proteomes; UP000001412; 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; 2.
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..6
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00626"
FT                   /id="PRO_0000026876"
FT   CHAIN           7..323
FT                   /note="Germination protease"
FT                   /id="PRO_0000026877"
SQ   SEQUENCE   323 AA;  35678 MW;  4833F5E96EAF090B CRC64;
     MSVRTDLAVE AKEIYEEKNA GEIPGVELKE YRQGRIKVTE VNVLNEQGEK AMNKAIGNYI
     TLEIPDINQY DTQYKEHISK ILAKTLMPLL KIDDSMTALV VGLGNWNITP DALGPKVIEK
     IMITRHLKEY IPNEIDEGIR PVCGISPGVL GITGIETAEI IKAVSNKIKP DIILCIDALA
     SRRLERVNRT IQIGNTGISP GAGVGNRRME LNEKTLGVPV IAIGVPTVVD AATVANDTID
     MVLDEMIKVA DKDKNFYNML KSLDRDEKER MIKEVLNPYV GELMVTPKDV DTLMDSISKI
     ISTGINIALQ PALELEDINS YLN