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Protein

Germination protease

Gene

gpr

Organism
Bacillus megaterium (strain ATCC 12872 / QMB1551)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

BioCyciBMEG545693:GHSY-4571-MONOMER.
BRENDAi3.4.24.78. 656.

Protein family/group databases

MEROPSiA25.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Germination protease (EC:3.4.24.78)
Alternative name(s):
GPR endopeptidase
Germination proteinase
Spore protease
Gene namesi
Name:gpr
Ordered Locus Names:BMQ_4571
OrganismiBacillus megaterium (strain ATCC 12872 / QMB1551)
Taxonomic identifieri545693 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000000935 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 15151 PublicationPRO_0000026868Add
BLAST
Chaini16 – 370355Germination proteasePRO_0000026869Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Zymogen

Expressioni

Developmental stagei

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

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi545693.BMQ_4571.

Structurei

Secondary structure

1
370
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 279Combined sources
Beta strandi43 – 519Combined sources
Beta strandi54 – 618Combined sources
Helixi63 – 664Combined sources
Turni67 – 704Combined sources
Beta strandi74 – 807Combined sources
Beta strandi84 – 896Combined sources
Helixi90 – 10516Combined sources
Beta strandi114 – 1185Combined sources
Beta strandi122 – 1243Combined sources
Helixi125 – 1273Combined sources
Helixi129 – 1357Combined sources
Helixi141 – 1466Combined sources
Beta strandi158 – 1614Combined sources
Helixi164 – 1663Combined sources
Helixi173 – 18412Combined sources
Beta strandi187 – 1959Combined sources
Helixi200 – 2023Combined sources
Beta strandi203 – 2108Combined sources
Beta strandi218 – 2214Combined sources
Beta strandi226 – 2294Combined sources
Beta strandi245 – 2517Combined sources
Beta strandi254 – 2563Combined sources
Helixi260 – 2634Combined sources
Turni264 – 2685Combined sources
Helixi315 – 3228Combined sources
Beta strandi330 – 3345Combined sources
Helixi337 – 35216Combined sources
Helixi353 – 3564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C8BX-ray3.00A/B1-370[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22321.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A25 family.Curated

Phylogenomic databases

HOGENOMiHOG000058956.
KOiK06012.
OMAiVTRHLFK.

Family and domain databases

Gene3Di3.40.50.1450. 2 hits.
HAMAPiMF_00626. Germination_prot.
InterProiIPR023430. Pept_HybD-like_dom.
IPR005080. Peptidase_A25.
[Graphical view]
PfamiPF03418. Peptidase_A25. 1 hit.
[Graphical view]
PIRSFiPIRSF019549. Peptidase_A25. 1 hit.
SUPFAMiSSF53163. SSF53163. 1 hit.
TIGRFAMsiTIGR01441. GPR. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22321-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKELDLSQY SVRTDLAVEA KDIALENQPK PNNQSEIKGV IVKEKEEQGV
60 70 80 90 100
KISMVEITEE GAEAIGKKKG RYVTLESVGI REQDTEKQEA MEEVFAKELN
110 120 130 140 150
FFIKSLNIPD DASCLVVGLG NLSVTPDALG PKAVDNLLIT RHLFELQPES
160 170 180 190 200
VQDGFRPVSA IVPGVMGMTG IETSDIIFGV VKKVNPDFII AIDALAARSI
210 220 230 240 250
ERVNATIQIS DSGIHPGSGV GNKRKEISYE TLGIPVIAIG IPTVVDAVSI
260 270 280 290 300
TSDTIDFILK HFGREMKEQG KPSKSLLPSG MTFGEKKKLT EDDLPNEEQR
310 320 330 340 350
QTYLGMIGTL PDEEKRRLIH EVLAPLGHNL MVTPKEVDMF IEDMANVVAG
360 370
GLNAALHHEV DQENFGAYTH
Length:370
Mass (Da):40,497
Last modified:August 10, 2010 - v2
Checksum:iF235C361792C37EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891E → EE in AAA22499 (PubMed:1840582).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55262 Genomic DNA. Translation: AAA22499.1.
CP001983 Genomic DNA. Translation: ADE71575.1.
PIRiA39198.
RefSeqiWP_013059248.1. NC_014019.1.

Genome annotation databases

EnsemblBacteriaiADE71575; ADE71575; BMQ_4571.
KEGGibmq:BMQ_4571.
PATRICi35485914. VBIBacMeg35839_4612.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55262 Genomic DNA. Translation: AAA22499.1.
CP001983 Genomic DNA. Translation: ADE71575.1.
PIRiA39198.
RefSeqiWP_013059248.1. NC_014019.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C8BX-ray3.00A/B1-370[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi545693.BMQ_4571.

Protein family/group databases

MEROPSiA25.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADE71575; ADE71575; BMQ_4571.
KEGGibmq:BMQ_4571.
PATRICi35485914. VBIBacMeg35839_4612.

Phylogenomic databases

HOGENOMiHOG000058956.
KOiK06012.
OMAiVTRHLFK.

Enzyme and pathway databases

BioCyciBMEG545693:GHSY-4571-MONOMER.
BRENDAi3.4.24.78. 656.

Miscellaneous databases

EvolutionaryTraceiP22321.

Family and domain databases

Gene3Di3.40.50.1450. 2 hits.
HAMAPiMF_00626. Germination_prot.
InterProiIPR023430. Pept_HybD-like_dom.
IPR005080. Peptidase_A25.
[Graphical view]
PfamiPF03418. Peptidase_A25. 1 hit.
[Graphical view]
PIRSFiPIRSF019549. Peptidase_A25. 1 hit.
SUPFAMiSSF53163. SSF53163. 1 hit.
TIGRFAMsiTIGR01441. GPR. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF ZYMOGEN P46.

Entry informationi

Entry nameiGPR_BACMQ
AccessioniPrimary (citable) accession number: P22321
Secondary accession number(s): D5DSW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 10, 2010
Last modified: February 17, 2016
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.