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UniProtKB/Swiss-Prot entry P22322


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GPR_BACSU
Primary accession number P22322
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on August 1, 1991 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 69)
Name and origin of the protein
Protein name Germination protease [Precursor]
Synonyms EC 3.4.24.78
Spore protease
GPR endopeptidase
Germination proteinase
Gene name
Name: gpr
OrderedLocusNames: BSU25540
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=1840582 [NCBI, ExPASy, EBI, Israel, Japan]
Sussman M.D., Setlow P.;
"Cloning, nucleotide sequence, and regulation of the Bacillus subtilis gpr gene, which codes for the protease that initiates degradation of small, acid-soluble proteins during spore germination.";
J. Bacteriol. 173:291-300(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / JH642;
PubMed=8969508 [NCBI, ExPASy, EBI, Israel, Japan]
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.;
"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes.";
Microbiology 142:3103-3111(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[4]
PROTEIN SEQUENCE OF 1-6 AND 17-23.
PubMed=8478323 [NCBI, ExPASy, EBI, Israel, Japan]
Sanchez-Salas J.-L., Setlow P.;
"Proteolytic processing of the protease which initiates degradation of small, acid-soluble proteins during germination of Bacillus subtilis spores.";
J. Bacteriol. 175:2568-2577(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-368.
STRAIN=168 / JH642;
Takemaru K., Sato T., Kobayashi Y.;
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
Comments
  • FUNCTION: Initiates the degradation of small, acid-soluble proteins during spore germination.
  • CATALYTIC ACTIVITY: Endopeptidase action with P4 Glu or Asp, P1 preferably Glu > Asp, P1' hydrophobic and P2' Ala.
  • SUBUNIT: Homotetramer.
  • DEVELOPMENTAL STAGE: GPR transcription occurs during sporulation in forespore first by sigma-F and then by sigma-G.
  • PTM: Autoproteolytically processed. The inactive tetrameric zymogen termed p46 autoprocesses to a smaller form termed p41, which is active only during spore germination.
  • SIMILARITY: Belongs to the peptidase A25 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M55263; AAA22500.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D84432; BAA12457.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99117; CAB14496.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D17650; BAA04541.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B39198; B39198.
RefSeq NP_390432.1; -.
3D structure databases
HSSP P22321; 1C8B. [HSSP ENTRY / PDB]
ModBase P22322.
Protein family/group databases
MEROPS A25.001; -.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2550-MON; -.
Organism-specific databases
SubtiList BG10438; gpr. [Micado]
Ontologies
GO
GO:0004222; Molecular function: metalloendopeptidase activity (inferred from electronic annotation from HAMAP).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from HAMAP).
GO:0009847; Biological process: spore germination (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00626; -; 1.
PBIL [Tree]
InterPro IPR005080; Peptidase_A25.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.10100; Peptidase_A25; 1.
Pfam PF03418; Peptidase_A25; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF019549; Peptidase_A25; 1.
ProDom PD041835; Peptidase_A25; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01441; GPR; 1.
ProtoNet P22322.
Genome annotation databases
GeneID 937838; -.
GenomeReviews AL009126_GR; BSU25540.
KEGG bsu:BSU25540; -.
NMPDR fig|224308.1.peg.2557; -.
Phylogenomic databases
HOGENOM P22322; -.
Genome annotation databases
CMR P22322; BSU25540.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Hydrolase; Protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
PROPEP   1    16  16      PRO_0000026870
CHAIN   17   368  352     Germination protease. PRO_0000026871
Sequence information
Length: 368 AA [This is the length of the unprocessed precursor] Molecular weight: 40283 Da [This is the MW of the unprocessed precursor] CRC64: 7F69F6739199CA43 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKSELDVNQ YLIRTDLAVE TKEAMANQQA VPTKEIKGFI EKERDHGGIK IRTVDVTKEG 

        70         80         90        100        110        120 
AELSGKKEGR YLTLEAQGIR ENDSEMQEKV SAVFAEEFSA FLENLNISKD ASCLIVGLGN 

       130        140        150        160        170        180 
WNVTPDALGP MAVENLLVTR HLFKLQPENV QEGYRPVSAF APGVMGITGI ETSDIIKGVI 

       190        200        210        220        230        240 
EQSKPDFVIA IDALAARAVE RVNTTIQISD TGIHPGSGVG NKRKDLSKDT LGVPVIAIGV 

       250        260        270        280        290        300 
PTVVDAVTIA SDTVDYILKH FGREMKDNRP SRSLVPAGMT FGKKKVLTED DLPDQKQRQS 

       310        320        330        340        350        360 
FLGIVGTLQE DEKRQLIHEV LSPLGHNLMV TPKEVDSFID DMANVLANGL NTALHEKVSQ 


ENKGSYNH 

P22322 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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