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Information on EC 3.4.24.85 - S2P endopeptidase and Organism(s) Escherichia coli and UniProt Accession P0AEH1

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.85 S2P endopeptidase
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This record set is specific for:
Escherichia coli
UNIPROT: P0AEH1 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
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Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site DRSR_ILL_483-/-CVLTFLCLSFNPLTSLLQWGGA, in which the membrane-spanning segment is underlined. The residues NP (bold), 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced.
Synonyms
sterol regulatory element binding protein, spoivfb, site-2 protease, intramembrane-cleaving protease, i-clip, sll0528, slr0643, sterol-regulated protease, site-2-protease, rv2869c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramembrane-cleaving protease
-
-
proteinase, sterol regulatory element-binding protein
-
-
-
-
site-1 protease
-
-
-
-
site-2 protease
SREBP cleavage activity
-
-
-
-
SREBP cysteine proteinase
-
-
-
-
SREBP proteinase
-
-
-
-
SREBP-1 proteinase
-
-
-
-
SREBP-2 proteinase
sterol regulatory element-binding proteinase
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-
-
-
sterol-regulated protease
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
167140-48-9
-
752251-31-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATF6 + H2O
?
show the reaction diagram
-
-
-
-
?
beta-lactamase signal peptide + H2O
?
show the reaction diagram
-
cleaves within the hydrophobic core at Pro12-Phe13. Cleavage of signal peptide requires a preceding processing of preproteins by Lep
-
-
?
MSIQHFRVALIPFFAAFCLPVFA + H2O
MSIQHFRVALIP + FFAAFCLPVFA
show the reaction diagram
-
-
-
-
?
RseA protein + H2O
?
show the reaction diagram
-
-
-
-
?
SREBP NH2-522 fragment + H2O
NH2-484 fragment + 38 aa fragment
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
beta-lactamase signal peptide + H2O
?
show the reaction diagram
-
cleaves within the hydrophobic core at Pro12-Phe13. Cleavage of signal peptide requires a preceding processing of preproteins by Lep
-
-
?
MSIQHFRVALIPFFAAFCLPVFA + H2O
MSIQHFRVALIP + FFAAFCLPVFA
show the reaction diagram
-
-
-
-
?
RseA protein + H2O
?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
a zinc metalloprotease
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
yaeL cloned
GenBank
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
transmembrane protein YaeL has the consensus metal-binding site
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
RseP introduces a cleavage into signal peptides after their signal peptidase-mediated liberation from preproteins. The enzyme is involved in degradation of remnant signal peptides left in the bacterial cytoplasmic membrane
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
x * 45000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 45000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D402N
abolished activity
E23Q
abolished activity
H22F
abolished activity
H26F
abolished activity
H22F
-
active site mutant
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in pKK10 and pKK11 plasmid
expressed in pKK6
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kanehara, K.; Akiyama, Y.; Ito, K.
Characterization of the yaeL gene product and its S2P-protease motifs in Escherichia coli
Gene
281
71-79
2001
Escherichia coli (P0AEH1), Escherichia coli
Manually annotated by BRENDA team
Kanehara, K.; Ito, K.; Akiyama, Y.
YaeL (EcfE) activates the sigma(E) pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA
Genes Dev.
16
2147-2155
2002
Escherichia coli (P0AEH1), Escherichia coli
Manually annotated by BRENDA team
King-Lyons, N.D.; Smith, K.F.; Connell, T.D.
Expression of hurP, a gene encoding a prospective site 2 protease, is essential for heme-dependent induction of bhuR in Bordetella bronchiseptica
J. Bacteriol.
189
6266-6275
2007
Bordetella bronchiseptica, Escherichia coli, Vibrio cholerae serotype O1, Bordetella bronchiseptica RB50
Manually annotated by BRENDA team
Makinoshima, H.; Glickman, M.S.
Site-2 proteases in prokaryotes: regulated intramembrane proteolysis expands to microbial pathogenesis
Microbes Infect.
8
1882-1888
2006
Bacillus subtilis, Caulobacter vibrioides, Escherichia coli, Enterococcus faecalis, Mycobacterium tuberculosis, Vibrio cholerae serotype O1
Manually annotated by BRENDA team
Kinch, L.N.; Ginalski, K.; Grishin, N.V.
Site-2 protease regulated intramembrane proteolysis: Sequence homologs suggest an ancient signaling cascade
Protein Sci.
15
84-93
2006
Synechocystis sp., Arabidopsis thaliana, Halalkalibacterium halodurans, Caenorhabditis elegans, Deinococcus radiodurans, Drosophila melanogaster, Escherichia coli, Giardia intestinalis, Halobacterium sp., Homo sapiens, Methanothermobacter thermautotrophicus, Mycobacterium leprae, Plasmodium falciparum, Pyrobaculum aerophilum, Thermoplasma volcanium, Thermotoga maritima, Treponema pallidum
Manually annotated by BRENDA team
Chen, G.; Zhang, X.
New insights into S2P signaling cascades: regulation, variation and conservation
Protein Sci.
19
2015-2030
2010
Bordetella bronchiseptica, Bacillus subtilis, Caulobacter vibrioides, Cryptococcus neoformans, Escherichia coli, Enterococcus faecalis, Homo sapiens, Methanocaldococcus jannaschii, Mycobacterium tuberculosis, Pseudomonas aeruginosa, Streptococcus uberis
Manually annotated by BRENDA team
Saito, A.; Hizukuri, Y.; Matsuo, E.; Chiba, S.; Mori, H.; Nishimura, O.; Ito, K.; Akiyama, Y.
Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria
Proc. Natl. Acad. Sci. USA
108
13740-13745
2011
Bacillus subtilis, Escherichia coli
Manually annotated by BRENDA team