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P22321 (GPR_BACMQ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Germination protease

EC=3.4.24.78
Alternative name(s):
GPR endopeptidase
Germination proteinase
Spore protease
Gene names
Name:gpr
Ordered Locus Names:BMQ_4571
OrganismBacillus megaterium (strain ATCC 12872 / QMB1551) [Complete proteome] [HAMAP]
Taxonomic identifier545693 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Initiates the rapid degradation of small, acid-soluble proteins during spore germination. HAMAP MF_00626

Catalytic activity

Endopeptidase action with P4 Glu or Asp, P1 preferably Glu > Asp, P1' hydrophobic and P2' Ala. HAMAP MF_00626

Subunit structure

Homotetramer.

Developmental stage

GPR transcription occurs during sporulation in forespore first by sigma-F and then by sigma-G. HAMAP MF_00626

Post-translational modification

Autoproteolytically processed. The inactive tetrameric zymogen termed p46 autoprocesses to a smaller form termed p41, which is active only during spore germination. HAMAP MF_00626

Sequence similarities

Belongs to the peptidase A25 family.

Ontologies

Keywords
   Molecular functionHydrolase
Protease
   PTMZymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

spore germination

Inferred from electronic annotation. Source: InterPro

   Molecular functionpeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1515 HAMAP MF_00626
PRO_0000026868
Chain16 – 370355Germination protease HAMAP MF_00626
PRO_0000026869

Experimental info

Sequence conflict891E → EE in AAA22499. Ref.1

Secondary structure

..................................................... 370
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22321 [UniParc].

Last modified August 10, 2010. Version 2.
Checksum: F235C361792C37EC

FASTA37040,497
        10         20         30         40         50         60 
MEKELDLSQY SVRTDLAVEA KDIALENQPK PNNQSEIKGV IVKEKEEQGV KISMVEITEE 

        70         80         90        100        110        120 
GAEAIGKKKG RYVTLESVGI REQDTEKQEA MEEVFAKELN FFIKSLNIPD DASCLVVGLG 

       130        140        150        160        170        180 
NLSVTPDALG PKAVDNLLIT RHLFELQPES VQDGFRPVSA IVPGVMGMTG IETSDIIFGV 

       190        200        210        220        230        240 
VKKVNPDFII AIDALAARSI ERVNATIQIS DSGIHPGSGV GNKRKEISYE TLGIPVIAIG 

       250        260        270        280        290        300 
IPTVVDAVSI TSDTIDFILK HFGREMKEQG KPSKSLLPSG MTFGEKKKLT EDDLPNEEQR 

       310        320        330        340        350        360 
QTYLGMIGTL PDEEKRRLIH EVLAPLGHNL MVTPKEVDMF IEDMANVVAG GLNAALHHEV 

       370 
DQENFGAYTH 

« Hide

References

« Hide 'large scale' references
[1]"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."
Sussman M.D., Setlow P.
J. Bacteriol. 173:291-300(1991) [PubMed: 1840582] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 16-31.
[2]"Genome sequences of the industrial vitamin B12-producers B. megaterium QM B1551 and DSM319 reveal new insights into the Bacillus genome evolution and pan-genome structure."
Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., Vary P.S.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12872 / QMB1551.
[3]"Structure and mechanism of action of the protease that degrades small, acid-soluble spore proteins during germination of spores of Bacillus species."
Nessi C., Jedrzejas M.J., Setlow P.
J. Bacteriol. 180:5077-5084(1998) [PubMed: 9748439] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Crystal structure of a novel germination protease from spores of Bacillus megaterium: structural arrangement and zymogen activation."
Ponnuraj K., Rowland S., Nessi C., Setlow P., Jedrzejas M.J.
J. Mol. Biol. 300:1-10(2000) [PubMed: 10864493] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF ZYMOGEN P46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55262 Genomic DNA. Translation: AAA22499.1.
CP001983 Genomic DNA. Translation: ADE71575.1.
PIRA39198.
RefSeqYP_003565009.1. NC_014019.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C8BX-ray3.00A/B1-370[»]
ModBaseSearch...

Protein family/group databases

MEROPSA25.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000391700; EBBACP00000384501; EBBACG00000392381.
GeneID8989009.
GenomeReviewsGene locus BMQ_4571 in contig CP001983_GR.
KEGGbmq:BMQ_4571.
PATRIC35485914. VBIBacMeg35839_4612.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000001716.
ProtClustDBPRK02858.

Family and domain databases

HAMAPMF_00626. Germination_prot.
[Tree]
InterProIPR023430. Pept_HybD-like_dom.
IPR005080. Peptidase_A25.
[Graphical view]
Gene3DG3DSA:3.40.50.1450. Peptidase_A31. 2 hits.
KOK06012.
PfamPF03418. Peptidase_A25. 1 hit.
[Graphical view]
PIRSFPIRSF019549. Peptidase_A25. 1 hit.
SUPFAMSSF53163. SSF53163. 1 hit.
TIGRFAMsTIGR01441. GPR. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGPR_BACMQ
AccessionPrimary (citable) accession number: P22321
Secondary accession number(s): D5DSW3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 10, 2010
Last modified: January 25, 2012
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families