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Information on EC 3.4.21.B49 - ctpB peptidase
for references in articles please use BRENDA:EC3.4.21.B49
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Old data from external sources may still be available.
Please check here for current data: EC unknown
Please check here for current data: EC unknown
preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.B49 ctpB peptidase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
At3g57680, CtpB, yviB gene product, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CtpB
yviB gene product
CtpB
-
PDZ-containing carboxy-terminal processing serine protease with similar organization as SpoIVB
CtpB
-
PDZ-containing serine protease with similar organization as SpoIVB, enzyme activated by autoproteolysis and cleavage by SpoIVB
CtpB
-
serine protease with a domain structure that resembles those of SpoIVB
CtpB
-
PDZ-containing carboxy-terminal processing serine protease with similar organization as SpoIVB
-
CtpB
-
PDZ-containing serine protease with similar organization as SpoIVB, enzyme activated by autoproteolysis and cleavage by SpoIVB
-
CtpB
-
serine protease with a domain structure that resembles those of SpoIVB
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
involved in sigmaK signaling, acts in cooperation with SpoIVB
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GFP-delta27 BofA + H2O
?
-
Substrates: -
Products: one or two low molecular weight species detected
Products: one or two low molecular weight species detected
?
His tagged extracellular domain of SpoIVFA + H2O
?
-
Substrates: two cleavage sites identified, cleavage sites different from those of SpoIVB
Products: -
Products: -
?
BofA + H2O
fragments of BofA
-
Substrates: involved in sigmaK signaling, acts in cooperation with SpoIVB, substrate and enzyme coexpressed in Escherichia coli, cleavage site near the C-terminus
Products: -
Products: -
?
BofA + H2O
fragments of BofA
-
Substrates: involved in sigmaK signaling, acts in cooperation with SpoIVB, substrate and enzyme coexpressed in Escherichia coli, cleavage site near the C-terminus
Products: -
Products: -
?
BofA + H2O
fragments of BofA
-
Substrates: involved in sigmaK signaling, acts in cooperation with SpoIVB, substrate and enzyme coexpressed in Escherichia coli, cleavage site near the C-terminus
Products: -
Products: -
?
SpoIVFA + H2O
fragements of SpoIVFA
-
Substrates: enzyme can substitute the function of SpoIVB, involved in sigmaK processing
Products: -
Products: -
?
SpoIVFA + H2O
fragements of SpoIVFA
-
Substrates: enzyme can substitute the function of SpoIVB, involved in sigmaK processing
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cannot process the C-terminal extension of the D1 precursor in vitro
Products: -
Products: -
-
additional information
?
-
-
Substrates: autoproteolysis as observed for SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: no effect on SpoIVFA when coexpressed in Escherichia coli
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in sigmaK signaling, acts in cooperation with SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: autoproteolysis as observed for SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the fine tuning of sigmaK signaling, acts in cooperation with SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleavage of BofA not detectable in an in vitro assay
Products: -
Products: -
?
additional information
?
-
-
Substrates: autoproteolysis as observed for SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in sigmaK signaling, acts in cooperation with SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: autoproteolysis as observed for SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: autoproteolysis as observed for SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the fine tuning of sigmaK signaling, acts in cooperation with SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cannot process the C-terminal extension of the D1 precursor in vitro
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme cannot process the C-terminal extension of the D1 precursor in vitro
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
BofA + H2O
fragments of BofA
-
Substrates: involved in sigmaK signaling, acts in cooperation with SpoIVB, substrate and enzyme coexpressed in Escherichia coli, cleavage site near the C-terminus
Products: -
Products: -
?
BofA + H2O
fragments of BofA
-
Substrates: involved in sigmaK signaling, acts in cooperation with SpoIVB, substrate and enzyme coexpressed in Escherichia coli, cleavage site near the C-terminus
Products: -
Products: -
?
BofA + H2O
fragments of BofA
-
Substrates: involved in sigmaK signaling, acts in cooperation with SpoIVB, substrate and enzyme coexpressed in Escherichia coli, cleavage site near the C-terminus
Products: -
Products: -
?
SpoIVFA + H2O
fragements of SpoIVFA
-
Substrates: enzyme can substitute the function of SpoIVB, involved in sigmaK processing
Products: -
Products: -
?
SpoIVFA + H2O
fragements of SpoIVFA
-
Substrates: enzyme can substitute the function of SpoIVB, involved in sigmaK processing
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cannot process the C-terminal extension of the D1 precursor in vitro
Products: -
Products: -
-
additional information
?
-
-
Substrates: autoproteolysis as observed for SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: no effect on SpoIVFA when coexpressed in Escherichia coli
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in sigmaK signaling, acts in cooperation with SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: autoproteolysis as observed for SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the fine tuning of sigmaK signaling, acts in cooperation with SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: autoproteolysis as observed for SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in sigmaK signaling, acts in cooperation with SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: autoproteolysis as observed for SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: autoproteolysis as observed for SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the fine tuning of sigmaK signaling, acts in cooperation with SpoIVB
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cannot process the C-terminal extension of the D1 precursor in vitro
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme cannot process the C-terminal extension of the D1 precursor in vitro
Products: -
Products: -
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
secreted by the mother cell into the intermembrane space between the forespore and the mother cell membrane
brenda
-
secreted by the mother cell into the intermembrane space between the forespore and the mother cell membrane
-
brenda
additional information
-
secreted by the mother cell into the intermembrane space between the forespore and the mother cell membrane
-
brenda
additional information
-
secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane
-
brenda
additional information
-
intermembrane space between the forespore and the mother cell membrane
-
brenda
additional information
-
secreted by the mother cell into the intermembrane space between the forespore and the mother cell membrane
-
-
brenda
additional information
-
secreted by the forespore into the intermembrane space between the forespore and the mother cell membrane
-
-
brenda
additional information
-
secreted by the mother cell into the intermembrane space between the forespore and the mother cell membrane
-
-
brenda
additional information
-
intermembrane space between the forespore and the mother cell membrane
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme loss does not alter plant growth and D1 precursor processing in Arabidopsis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S309A
S309A
additional information
additional information
-
deletion mutant causes delay in the signaling process in vivo
additional information
-
deletion mutant causes delay in the signaling process in vivo
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhou, R.; Kroos, L.
Serine proteases from two cell types target different components of a complex that governs regulated intramembrane proteolysis of pro-sigmaK during Bacillus subtilis development
Mol. Microbiol.
58
835-846
2005
Bacillus subtilis, Bacillus subtilis PY79
brenda
Pan, Q.; Losick, R.; Rudner, D.Z.
A second PDZ-containing serine protease contributes to activation of the sporulation transcription factor sigmaK in Bacillus subtilis
J. Bacteriol.
185
6051-6056
2003
Bacillus subtilis, Bacillus subtilis PY79
brenda
Campo N.; Rudner D.Z.
SpoIVB and CtpB are both forespore signals in the activation of the sporulation transcription factor sigmaK in Bacillus subtilis
J. Bacteriol.
189
6021-6027
2007
Bacillus subtilis, Bacillus subtilis PY79
brenda
Campo, N.; Rudner, D.Z.
A branched pathway governing the activation of a developmental transcription factor by regulated intramembrane proteolysis
Mol. Cell
23
25-35
2006
Bacillus subtilis, Bacillus subtilis PY79
brenda
Chang, W.; Li, C.; Cui, Z.; Li, W.; Song, H.; Chang, H.; Fu, W.; Wang, C.; Huang, T.; Luo, Y.; Shan, Y.; Wang, Y.; Wang, F.; Xu, M.; Fu, A.
Diverged early from CtpB and CtpC, CtpA has evolved to process D1 precursor in oxygenic photosynthetic organisms
Front. Plant Sci.
12
676036
2021
Arabidopsis thaliana, Chlamydomonas reinhardtii, Physcomitrium patens
brenda
EXTERNAL LINKS (specific for EC-Number 3.4.21.B49)
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