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Information on EC 3.4.21.53 - Endopeptidase La and Organism(s) Bacillus subtilis and UniProt Accession P37945

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.53 Endopeptidase La
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This record set is specific for:
Bacillus subtilis
UNIPROT: P37945 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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hydrolysis of proteins in presence of ATP
Synonyms
protease, serine protease, clpxp, lon protease, lonp1, protease la, atp-dependent lon protease, protease lon, aaa+ protease, ms-lon, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP-dependent Lon proteinase
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ATP-dependent protease La
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ATP-dependent serine proteinase
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Escherichia coli proteinase La
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Escherichia coli serine proteinase La
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Gene lon protease
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Gene lon proteins
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lon ATP-dependent protease
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Lon proteinase
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PIM1 protease
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PIM1 proteinase
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Protease La
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Proteinase La
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Proteinase, Escherichia coli serine, La
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Proteinase, La
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Proteins, gene lon
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Proteins, specific or class, gene lon
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Serine protease La
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CAS REGISTRY NUMBER
COMMENTARY hide
79818-35-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
sigma factor G + H2O
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show the reaction diagram
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lonA
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?
sigma factor H + H2O
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show the reaction diagram
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lonA
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?
SMC protein + H2O
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show the reaction diagram
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lonA
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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substrate specificity of isoforms LonA, LonB and of protease Clp can be determined, in part, by the spatial and temporal organization of the proteases in vivo
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?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
puromycin
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additional information
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lonA gene is induced by heat and salt, lonB is not stress-induced
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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lonA is involved in the control of sporulation initiation, lonB is only present in the forespore
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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isoform LonA, during development. Isoform LonB localizes to the forespore membrane early in development, followed by localization throughout the forespore later in development
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Manually annotated by BRENDA team
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isoform LonA, during normal growth
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
87400
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 87400, calculated. Mixture of monomeric and larger oligomeric species, with increasing amounts of larger oligomers present at larger concentrations
oligomer
x * 87400, calculated. Mixture of monomeric and larger oligomeric species, with increasing amounts of larger oligomers present at larger concentrations
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fragment containing the ATPase and protease domains, to 3.4 A resolution. The C-terminal protease domain and the two ATPase sub-domains, form a three-lobed structure, whilst the fourth, the N-terminal domain of the fragment, protrudes from the side of the ATPase domain. A second fragment containing two-thirds of the N-terminal domain, to 2.6 A resolution, shows a domain-swapped dimer in the asymmetric unit. The structure of the N-terminal fragment consists of two distinct regions, connected by an extended loop of 10 amino acids: a compact beta-sheet rich, globular domain. Lon protease complexes may be stabilized by coiled-coil interactions between neighbouring N-terminal domains
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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lonB disruption does not affect sporulation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression as green fluorescent protein-fusion protein
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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lonA plays a major role in initiating sporulation in response to environmental conditions, lonB is forespore-specific and may have a limited role in the regulation of sporulation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsilibaris, V.; Maenhaut-Michel, G.; Van Melderen, L.
Biological roles of the Lon ATP-dependent protease
Res. Microbiol.
157
701-713
2006
Brevibacillus brevis, Bacillus subtilis, Saccharomyces cerevisiae, Caulobacter vibrioides, Escherichia coli, Homo sapiens, Myxococcus xanthus, no activity in Lactobacillus sp., no activity in Streptococcus sp., Yersinia pestis, Proteus mirabilis, Pseudomonas syringae, Salmonella enterica subsp. enterica serovar Typhimurium, Streptomyces lividans, Vibrio parahaemolyticus, no activity in Mycobacterium tuberculosis, no activity in Mycobacterium leprae
Manually annotated by BRENDA team
Simmons, L.A.; Grossman, A.D.; Walker, G.C.
Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis
J. Bacteriol.
190
6758-6768
2008
Bacillus subtilis
Manually annotated by BRENDA team
Lin, Y.C.; Lee, H.C.; Wang, I.; Hsu, C.H.; Liao, J.H.; Lee, A.Y.; Chen, C.; Wu, S.H.
DNA-binding specificity of the Lon protease alpha-domain from Brevibacillus thermoruber WR-249
Biochem. Biophys. Res. Commun.
388
62-66
2009
Bacillus subtilis, Escherichia coli, Brevibacillus thermoruber, Brevibacillus thermoruber WR-249
Manually annotated by BRENDA team
Duman, R.E.; Loewe, J.
Crystal structures of Bacillus subtilis Lon protease
J. Mol. Biol.
401
653-670
2010
Bacillus subtilis (P37945), Bacillus subtilis
Manually annotated by BRENDA team