ID   GPR_PRIM1               Reviewed;         370 AA.
AC   P22321; D5DSW3;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Germination protease;
DE            EC=3.4.24.78;
DE   AltName: Full=GPR endopeptidase;
DE   AltName: Full=Germination proteinase;
DE   AltName: Full=Spore protease;
DE   Flags: Precursor;
GN   Name=gpr; OrderedLocusNames=BMQ_4571;
OS   Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=545693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 16-31.
RX   PubMed=1840582; DOI=10.1128/jb.173.1.291-300.1991;
RA   Sussman M.D., Setlow P.;
RT   "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis gpr
RT   gene, which codes for the protease that initiates degradation of small,
RT   acid-soluble proteins during spore germination.";
RL   J. Bacteriol. 173:291-300(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551;
RX   PubMed=21705586; DOI=10.1128/jb.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=9748439; DOI=10.1128/jb.180.19.5077-5084.1998;
RA   Nessi C., Jedrzejas M.J., Setlow P.;
RT   "Structure and mechanism of action of the protease that degrades small,
RT   acid-soluble spore proteins during germination of spores of Bacillus
RT   species.";
RL   J. Bacteriol. 180:5077-5084(1998).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF ZYMOGEN P46.
RX   PubMed=10864493; DOI=10.1006/jmbi.2000.3849;
RA   Ponnuraj K., Rowland S., Nessi C., Setlow P., Jedrzejas M.J.;
RT   "Crystal structure of a novel germination protease from spores of Bacillus
RT   megaterium: structural arrangement and zymogen activation.";
RL   J. Mol. Biol. 300:1-10(2000).
CC   -!- FUNCTION: Initiates the rapid degradation of small, acid-soluble
CC       proteins during spore germination.
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   -!- SUBUNIT: Homotetramer.
CC   -!- DEVELOPMENTAL STAGE: GPR transcription occurs during sporulation in
CC       forespore first by sigma-F and then by sigma-G.
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.
CC   -!- SIMILARITY: Belongs to the peptidase A25 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M55262; AAA22499.1; -; Genomic_DNA.
DR   EMBL; CP001983; ADE71575.1; -; Genomic_DNA.
DR   PIR; A39198; A39198.
DR   RefSeq; WP_013059248.1; NC_014019.1.
DR   PDB; 1C8B; X-ray; 3.00 A; A/B=1-370.
DR   PDBsum; 1C8B; -.
DR   AlphaFoldDB; P22321; -.
DR   SMR; P22321; -.
DR   STRING; 545693.BMQ_4571; -.
DR   MEROPS; A25.001; -.
DR   EnsemblBacteria; ADE71575; ADE71575; BMQ_4571.
DR   KEGG; bmq:BMQ_4571; -.
DR   eggNOG; COG0680; Bacteria.
DR   HOGENOM; CLU_055087_1_0_9; -.
DR   OMA; PMGNYIT; -.
DR   OrthoDB; 799376at2; -.
DR   BRENDA; 3.4.24.78; 656.
DR   EvolutionaryTrace; P22321; -.
DR   Proteomes; UP000000935; 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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Protease;
KW   Reference proteome; Zymogen.
FT   PROPEP          1..15
FT                   /evidence="ECO:0000269|PubMed:1840582"
FT                   /id="PRO_0000026868"
FT   CHAIN           16..370
FT                   /note="Germination protease"
FT                   /id="PRO_0000026869"
FT   CONFLICT        89
FT                   /note="E -> EE (in Ref. 1; AAA22499)"
FT                   /evidence="ECO:0000305"
FT   HELIX           19..27
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          43..51
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          54..61
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           63..66
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   TURN            67..70
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          74..80
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          84..89
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           90..105
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          114..118
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           129..135
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           141..146
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          158..161
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           173..184
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          187..195
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           200..202
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          203..210
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          218..221
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          226..229
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          245..251
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           260..263
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   TURN            264..268
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           315..322
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   STRAND          330..334
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           337..352
FT                   /evidence="ECO:0007829|PDB:1C8B"
FT   HELIX           353..356
FT                   /evidence="ECO:0007829|PDB:1C8B"
SQ   SEQUENCE   370 AA;  40497 MW;  F235C361792C37EC CRC64;
     MEKELDLSQY SVRTDLAVEA KDIALENQPK PNNQSEIKGV IVKEKEEQGV KISMVEITEE
     GAEAIGKKKG RYVTLESVGI REQDTEKQEA MEEVFAKELN FFIKSLNIPD DASCLVVGLG
     NLSVTPDALG PKAVDNLLIT RHLFELQPES VQDGFRPVSA IVPGVMGMTG IETSDIIFGV
     VKKVNPDFII AIDALAARSI ERVNATIQIS DSGIHPGSGV GNKRKEISYE TLGIPVIAIG
     IPTVVDAVSI TSDTIDFILK HFGREMKEQG KPSKSLLPSG MTFGEKKKLT EDDLPNEEQR
     QTYLGMIGTL PDEEKRRLIH EVLAPLGHNL MVTPKEVDMF IEDMANVVAG GLNAALHHEV
     DQENFGAYTH