(data stored in SCRATCH zone)

SWISSPROT: GPR_BACSU

ID   GPR_BACSU               Reviewed;         368 AA.
AC   P22322;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   11-DEC-2019, entry version 133.
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=BSU25540;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
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 [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-6 AND 17-23.
RX   PubMed=8478323; DOI=10.1128/jb.175.9.2568-2577.1993;
RA   Sanchez-Salas J.-L., Setlow P.;
RT   "Proteolytic processing of the protease which initiates degradation of
RT   small, acid-soluble proteins during germination of Bacillus subtilis
RT   spores.";
RL   J. Bacteriol. 175:2568-2577(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-368.
RC   STRAIN=168 / JH642;
RA   Takemaru K., Sato T., Kobayashi Y.;
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Initiates the degradation of small, acid-soluble proteins
CC       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}.
DR   EMBL; M55263; AAA22500.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12457.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14496.1; -; Genomic_DNA.
DR   EMBL; D17650; BAA04541.1; -; Genomic_DNA.
DR   PIR; B39198; B39198.
DR   RefSeq; NP_390432.1; NC_000964.3.
DR   RefSeq; WP_003229991.1; NZ_JNCM01000036.1.
DR   STRING; 224308.BSU25540; -.
DR   MEROPS; A25.001; -.
DR   PaxDb; P22322; -.
DR   PRIDE; P22322; -.
DR   EnsemblBacteria; CAB14496; CAB14496; BSU25540.
DR   GeneID; 937838; -.
DR   KEGG; bsu:BSU25540; -.
DR   PATRIC; fig|224308.179.peg.2775; -.
DR   eggNOG; ENOG4105CEF; Bacteria.
DR   eggNOG; ENOG410XNXE; LUCA.
DR   HOGENOM; HOG000058956; -.
DR   KO; K06012; -.
DR   OMA; PMGNYIT; -.
DR   PhylomeDB; P22322; -.
DR   BioCyc; BSUB:BSU25540-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009847; P:spore germination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1450; -; 2.
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;
DR   PRODOM; P22322.
DR   SWISS-2DPAGE; P22322.
KW   Direct protein sequencing; Hydrolase; Protease; Reference proteome;
KW   Zymogen.
FT   PROPEP          1..16
FT                   /evidence="ECO:0000269|PubMed:8478323"
FT                   /id="PRO_0000026870"
FT   CHAIN           17..368
FT                   /note="Germination protease"
FT                   /id="PRO_0000026871"
SQ   SEQUENCE   368 AA;  40283 MW;  7F69F6739199CA43 CRC64;
     MKKSELDVNQ YLIRTDLAVE TKEAMANQQA VPTKEIKGFI EKERDHGGIK IRTVDVTKEG
     AELSGKKEGR YLTLEAQGIR ENDSEMQEKV SAVFAEEFSA FLENLNISKD ASCLIVGLGN
     WNVTPDALGP MAVENLLVTR HLFKLQPENV QEGYRPVSAF APGVMGITGI ETSDIIKGVI
     EQSKPDFVIA IDALAARAVE RVNTTIQISD TGIHPGSGVG NKRKDLSKDT LGVPVIAIGV
     PTVVDAVTIA SDTVDYILKH FGREMKDNRP SRSLVPAGMT FGKKKVLTED DLPDQKQRQS
     FLGIVGTLQE DEKRQLIHEV LSPLGHNLMV TPKEVDSFID DMANVLANGL NTALHEKVSQ
     ENKGSYNH
//

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