Any feedback?
No. of entries
Information on EC 3.4.21.102 - C-terminal processing peptidase
for references in articles please use BRENDA:EC3.4.21.102
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.102 C-terminal processing peptidase
IUBMB Comments
Proteolytic processing of the D1 protein of photosystem II is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation. The recognition of the substrate is mediated by a PDZ domain, a small protein module that promotes protein-protein interactions by binding to internal or C-terminal sequences of their partner proteins. Type example of peptidase family S41.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 3.4.21.102
-
krabbe
- thylakoids
-
leukodystrophy
-
globoid
-
twitcher
- psychosine
- galactosylceramide
-
photoinhibition
-
oxygen-evolving
- galactocerebroside
- agriculture
- drug development
Reaction Schemes
showthe enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
Synonyms
stromal processing peptidase, c-terminal protease, tail-specific protease, photosystem ii d1 protein, c-terminal processing protease, carboxyl-terminal processing protease, prc protein, carboxyl-terminal protease, photosystem ii protein d1, protease re, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C-terminal processing peptidase
-
-
-
-
C-terminal processing protease
carboxy terminal-processing proteinase
-
-
-
-
carboxyl-terminal processing protease
chloroplast processing enzyme
chloroplast protein precursor processing proteinase
-
-
-
-
CtpA
CtpA gene product
-
-
-
-
D1 preprotein-processing proteinase
-
-
-
-
D1 protein-processing enzyme
-
-
-
-
photosystem D1 protein precursor carboxyl-terminal processing protease
-
-
-
-
photosystem II D1 C-terminal processing protease
-
-
-
-
photosystem II D1 protein
-
-
-
-
photosystem II D1 protein processing proteinase
-
-
-
-
PrC
Prc protease
PRC protein
-
-
-
-
processing peptidase
-
-
-
-
protease Re
-
-
-
-
proteinase CtpA
-
-
-
-
proteinase, chloroplast protein precursor-processing
-
-
-
-
SPP
stromal processing peptidase
tail-specific protease
-
-
-
-
thylakoid protein precursor processing peptidase
-
-
-
-
Tsp protease
-
-
-
-
additional information
C-terminal processing protease
-
-
-
-
stromal processing peptidase
-
-
-
-
additional information
-
the enzyme probably belongs to the M16 peptidase family
additional information
O48870
the enzyme probably belongs to the M16 peptidase family
additional information
-
the enzyme probably belongs to the M16 peptidase family
additional information
-
the enzyme probably belongs to the M16 peptidase family
additional information
-
the enzyme probably belongs to the M16 peptidase family
additional information
-
the enzyme probably belongs to the M16 peptidase family
additional information
the enzyme probably belongs to the M16 peptidase family
additional information
-
the enzyme probably belongs to the M16 peptidase family
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
Proteolytic processing of the D1 protein of photosystem II is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation. The recognition of the substrate is mediated by a PDZ domain, a small protein module that promotes protein-protein interactions by binding to internal or C-terminal sequences of their partner proteins. Type example of peptidase family S41
-
-
-
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
mechanism, transit peptide binding and removal are two separable steps of the reaction
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
substrate recognition site is located between amino acids 206 and 334 where there is also a putative PDZ domain
-
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
light
-
-
-
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
reaction mechanism, process model, substrate recognition, overview
-
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
reaction mechanism, process model, substrate recognition, overview
-
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
reaction mechanism, process model, substrate recognition, overview
-
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
reaction mechanism, process model, substrate recognition, overview
-
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
reaction mechanism, process model, substrate recognition, overview
O48870
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
reaction mechanism, process model, substrate recognition, overview
-
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
reaction mechanism, process model, substrate recognition, overview
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
reaction mechanism, process model, substrate recognition, overview
the enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-/-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II
reaction mechanism, process model, substrate recognition, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
216484-75-2
-
92480-11-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala + H2O
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala + Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
-
Substrates: -
Products: -
Products: -
?
Arc repressor + H2O
?
-
Substrates: C-terminal sequence: GRIGA, endoproteolyric cleavage
Products: -
Products: -
?
C-terminal 19 amino acids of preD1 protein + H2O
pre-peptide of D1 + oligomer of 11 amino acids
-
Substrates: replacement of Ala at the cleaving site by Gly, Val, Pro reduces the rate of proteolysis to 50, 30 and 0% of the control
Products: -
Products: -
?
core protein S1 precursor + H2O
?
Substrates: -
Products: -
Products: -
?
cytochrome-b562-WVAAA + H2O
?
-
Substrates: cytochrome b562 with a C-terminal attachment, fast hydrolysis
Products: -
Products: -
?
cytochrome-b562-WVAAK + H2O
?
-
Substrates: cytochrome b562 with a C-terminal attachment, no hydrolysis
Products: -
Products: -
?
cytochrome-b562-WVAAV + H2O
?
-
Substrates: cytochrome b562 with a C-terminal attachment, slow hydrolysis
Products: -
Products: -
?
cytochrome-b562-WVAGA + H2O
?
-
Substrates: cytochrome b562 with a C-terminal attachment, slow hydrolysis
Products: -
Products: -
?
cytochrome-b562-WVAYA + H2O
?
-
Substrates: cytochrome b562 with a C-terminal attachment, fast hydrolysis
Products: -
Products: -
?
cytochrome-b562-WVLAA + H2O
?
-
Substrates: cytochrome b562 with a C-terminal attachment, fast hydrolysis
Products: -
Products: -
?
cytochrome-b562-WVQAA + H2O
?
-
Substrates: cytochrome b562 with a C-terminal attachment, slow hydrolysis
Products: -
Products: -
?
D1 protein precursor + H2O
mature D1 protein + ?
Substrates: -
Products: -
Products: -
?
maize preOEC17
OEC17 + presequence
-
Substrates: precursor of thylakoid lumen protein OEC17
Products: -
Products: -
?
P-24 peptide + H2O
?
Substrates: peptide substrate comprising the 24 C-terminal residues of spinach pre-D1 protein
Products: -
Products: -
?
photosystem II D1 protein + H2O
?
-
Substrates: specific substrate for enzyme form CtpB
Products: -
Products: -
?
pre-D1 protein + H2O
D1 protein + peptide
-
Substrates: catalyzes the conversion of the nascent pre-D1 (pD1) protein into the active form of D1 by cleaving the 9 C-terminal residues in spinach, required to maintain the function of the photosystem II complex
Products: -
Products: -
?
pre-LHCP protein + H2O
LHCP protein + transit peptide
Substrates: -
Products: -
Products: -
?
pre-RBCS protein + H2O
RBCS protein + transit peptide
-
Substrates: -
Products: -
Products: -
?
prePsbO + H2O
PsbO + presequence
-
Substrates: precursor of thylakoid lumen protein PsbO or OEC33
Products: -
Products: -
?
ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit precursor + H2O
?
-
Substrates: -
Products: -
Products: -
?
SpoIVFA + H2O
?
-
Substrates: specific substrate for enzyme form CtpA
Products: -
Products: -
?
anti-sigma factor MucA + H2O
?
-
Substrates: the Prc protease degrades mutants forms of MucA, the enzyme activity does not affect alginate production in strains with wild-type MucA, but MucA22 mutants show the mucoid phenotype, overview
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: -
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: -
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: enzymatic cleavage occurs on the C-terminal site of Ala344
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: investigation of substrate recognition sites
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: -
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: determination of the catalytic important residues
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: removal of the C-terminal extension
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: -
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: removal of the C-terminal extension
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: in vivo proteolytic processing of pre-D1, no other protease can compensate for its loss
Products: -
Products: -
?
D1 protein + H2O
?
Substrates: C-terminal processing of D1 protein
Products: -
Products: -
?
F-24 peptide + H2O
?
Substrates: peptide substrate comprising the 24 C-terminal residues of spinach pre-D1 protein, N-terminally fluorescence-labeled with a fluorescein isothiocyanate group
Products: -
Products: -
?
F-24 peptide + H2O
?
-
Substrates: peptide substrate comprising the 24 C-terminal residues of spinach pre-D1 protein, N-terminally fluorescence-labeled with a fluorescein isothiocyanate group
Products: -
Products: -
?
membrane protein SpoIVFA + H2O
?
Substrates: sequenctial processing by the enzyme together with protease 4B. The 4FA regulatory protein is composed of a globular N-terminal domain, a transmembrane helix (residues 73-90), an unstructured linker region and a compact C-terminal domain (residues 160-255, LytM-like) extending into the intermembrane space. 4B/CtpB-mediated removal of 4FA residues 131-154 induces sK maturation
Products: -
Products: -
?
NIpI protein + H2O
?
-
Substrates: processing of wild-type substrate and mutants lacking up to 11 amino acids of the C-terminus in vivo, a mutant NIpI protein lacking 12 C-terminal amino acids is not processed, overview, the enzyme activates the substrate
Products: -
Products: -
?
NIpI protein + H2O
?
-
Substrates: processing of wild-type substrate and mutants lacking up to 11 amino acids of the C-terminus, a mutant NIpI protein lacking 12 C-terminal amino acids is not processed, overview
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: Tsp is a component of the ssrA RNA protein-tagging pathway for the removal of incorrectly synthesized proteins
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal positions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third postion from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
Products: -
Products: -
?
SP-4 peptide + H2O
?
Substrates: peptide substrate comprising the 16 C-terminal residues of spinach pre-D1 protein with an inserted Lys between position 6 and 7 from the C-terminus, the Lys is fluorescence-labeled with a fluorescein isothiocyanate group at the epsilon-amino function, N-terminally biotin-labeled
Products: -
Products: -
?
SP-4 peptide + H2O
?
-
Substrates: peptide substrate comprising the 16 C-terminal residues of spinach pre-D1 protein with an inserted Lys between position 6 and 7 from the C-terminus, the Lys is fluorescence-labeled with a fluorescein isothiocyanate group at the epsilon-amino function, N-terminally biotin-labeled
Products: -
Products: -
?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
variant of the lambda repressor + H2O
?
-
Substrates: C-terminal sequence: WVAAA, endoproteolytic cleavage
Products: -
Products: -
?
variant of the lambda repressor + H2O
?
Substrates: C-terminal sequence: WVAAA, endoproteolytic cleavage
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate recognition by specific protein-protein interaction, endoprotease activity, overview
Products: -
Products: -
?
additional information
?
-
O48870
Substrates: broad substrate specificity, overview, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview, the enzyme is essential for plant survival, regulation of expression in vivo
Products: -
Products: -
?
additional information
?
-
O48870
Substrates: substrate recognition by specific protein-protein interaction, endoprotease activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the protease CtpB is active without the PDZ domain
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme belongs to the family of endoproteases involved in the maturation of proteins destined for the cell envelope
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate recognition by specific protein-protein interaction, endoprotease activity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
Substrates: substrate recognition by specific protein-protein interaction, endoprotease activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate recognition by specific protein-protein interaction, endoprotease activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate recognition by specific protein-protein interaction, endoprotease activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate recognition by specific protein-protein interaction, endoprotease activity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the apicoplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
Substrates: substrate recognition by specific protein-protein interaction, endoprotease activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: critical for the viability when cells are grown on complex semi-solid media, not essential when cells are grown in complex liquid media, enzyme function affects the permeability of the cell wall
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate recognition by specific protein-protein interaction, endoprotease activity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the geometry of the TyrZ phenol group and its environment, likely the Tyr-O-H-Nepsilon-His bonding, are modified in isoform PsbA2-PSII when compared with isoforms PsbA(1/3)-PSII. They also point to the dynamics of the proton-coupled electron transfer processes associated with the oxidation of TyrZ being affected. The C144P and P173M substitutions in isoform PsbA2-PSII versus PsbA(1/3)-PSII, respectively located upstream of the alpha-helix bearing TyrZ and between the two alpha-helices bearing TyrZ and its hydrogen-bonded partner, His-190, are responsible for these changes
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
anti-sigma factor MucA + H2O
?
-
Substrates: the Prc protease degrades mutants forms of MucA, the enzyme activity does not affect alginate production in strains with wild-type MucA, but MucA22 mutants show the mucoid phenotype, overview
Products: -
Products: -
?
D1 protein + H2O
?
Substrates: C-terminal processing of D1 protein
Products: -
Products: -
?
membrane protein SpoIVFA + H2O
?
Substrates: sequenctial processing by the enzyme together with protease 4B. The 4FA regulatory protein is composed of a globular N-terminal domain, a transmembrane helix (residues 73-90), an unstructured linker region and a compact C-terminal domain (residues 160-255, LytM-like) extending into the intermembrane space. 4B/CtpB-mediated removal of 4FA residues 131-154 induces sK maturation
Products: -
Products: -
?
NIpI protein + H2O
?
-
Substrates: processing of wild-type substrate and mutants lacking up to 11 amino acids of the C-terminus in vivo, a mutant NIpI protein lacking 12 C-terminal amino acids is not processed, overview, the enzyme activates the substrate
Products: -
Products: -
?
pre-D1 protein + H2O
D1 protein + peptide
-
Substrates: catalyzes the conversion of the nascent pre-D1 (pD1) protein into the active form of D1 by cleaving the 9 C-terminal residues in spinach, required to maintain the function of the photosystem II complex
Products: -
Products: -
?
pre-LHCP protein + H2O
LHCP protein + transit peptide
Substrates: -
Products: -
Products: -
?
pre-RBCS protein + H2O
RBCS protein + transit peptide
-
Substrates: -
Products: -
Products: -
?
ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit precursor + H2O
?
-
Substrates: -
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: -
Products: -
Products: -
?
D1 polypeptide of photosystem II + H2O
?
-
Substrates: in vivo proteolytic processing of pre-D1, no other protease can compensate for its loss
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: Tsp is a component of the ssrA RNA protein-tagging pathway for the removal of incorrectly synthesized proteins
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: endogenous cleavage of proteins with hydrophobic or nonpolar residues at their C-terminal postions. Ala is preferred at the C-terminus, Ala or Tyr at the penultimate position, and Ala or Leu at the third position from the end. The cleavage site specificity is broad, with Ala, Ser, Val, and to a lesser extent Ile, Leu, Lys or Arg, preferred at the P1 position, and these same residues plus Met, Tyr, or Trp in P1' position.
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
O48870
Substrates: broad substrate specificity, overview, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview, the enzyme is essential for plant survival, regulation of expression in vivo
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme belongs to the family of endoproteases involved in the maturation of proteins destined for the cell envelope
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the apicoplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: critical for the viability when cells are grown on complex semi-solid media, not essential when cells are grown in complex liquid media, enzyme function affects the permeability of the cell wall
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, the stromal processing peptidase has a function in the chloroplast import pathway by cleaving the N-terminal transit peptide of pre-proteins translocated from the cytosol, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
the enzyme contains a HXXEH zinc-binding motif, metalloendopeptidase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibitory: EDTA, EGTA, leupeptin, phenylmethylsulfonyl fluoride, iodoacetic acid
-
additional information
-
insensitive to leupeptin, Nalpha-p-tosyl-L-Lys chloromethyl ketone, 1,10-phenanthroline
-
additional information
-
insensitive to penem; not inhibitory: phenylmethylsulfonyl fluoride, diisopropyl fluorophosphate, chymostatin, penem, pepstatin A, 2-mercaptoethanol, N-ethylmaleimide, EDTA, 1,10-phenanthroline
-
additional information
-
oligopeptides with 24 residues corresponding to the substrate with replacements of Asp342
-
additional information
-
complex inhibitors belonging to the substance classes rhodanine dimer, ketoheterocycles, CF3 peptides, and imidazoles were studied, application of inhibitors to the leaves of Arabidopsis thaliana causes lesions, over expression of CtpA results in enhanced resistance to inhibitor treatment
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
GTP
-
the nucleotide hydrolyis probably provides energy necessary for unfolding of the D1 protein and its N-terminal 23-kDa fragments because both of these substrates contain large loops connecting trans-membrane helices that may hide proteolytic sites
additional information
a peptide ligand, which copurifies and cocrystallizes with CtpB, is observed at the entrance of the protease tunnel near the catalytic triad, its binding to the PDZ domain stimulates the protease activity
-
additional information
-
degradation of D1 protein of photosystem II is enhanced by more than 2.5fold following preillumination of thylakoids
-
additional information
-
degradation of D1 protein of photosystem II is enhanced by more than 2.5fold following preillumination of thylakoids
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Encephalomyelitis, Venezuelan Equine
Purification, crystallization and X-ray diffraction analysis of the C-terminal protease domain of Venezuelan equine encephalitis virus nsP2.
Epilepsy
Crystallization, high-resolution data collection and preliminary crystallographic analysis of Aura virus capsid protease and its complex with dioxane.
Infections
The lone S41 family C-terminal processing protease in Staphylococcus aureus is localized to the cell wall and contributes to virulence.
Prostatic Neoplasms
Coordinated Regulation of Polycomb Group Complexes through microRNAs in Cancer.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0044 - 0.0111
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
0.0044
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
-
wild-type enzyme
0.0095
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
-
mutant V229Q
0.0111
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
-
mutant V229E
additional information
additional information
steady-state kinetics of recombinant and native enzymes using two different assay methods, overview
-
additional information
additional information
-
steady-state kinetics of recombinant and native enzymes using two different assay methods, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
-
wild-type enzyme, mutants V229Q, V229E
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Spinacia oleracea
-
IC values in the micromolar range found for the effective inhibitors
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000007 - 0.000015
purified recombinant CtpA, substrates P-24 or F-24 peptides
additional information
additional information
development of a high-throughput screening assay method on microtiter plates
additional information
-
development of a high-throughput screening assay method on microtiter plates
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
synonym Gliocladium roseum, anamorph of Bionectria ochrdeuca
-
-
brenda
strain PCC 6803, ORFs SLL2008 and SLL2009 encoding the C- and N-terminal enzyme part, respectively
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme is not detected in the cytoplasm or in the membrane
-
brenda
-
synthesized in the cytosol and translocated to the lumenal space of the thylakoids
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
evolution
the enzyme CtpB belongs to the widespread family of PDZ-proteases
malfunction
-
enzyme loss results in the accumulation of pD1 in Arabidopsis. In the mutant SALK_056011, the loss of D1 maturation mainly affects the incorporation of photosystem II core protein CP43, an inner antenna binding protein, which functions in the association of light-harvesting complex II to photosystem II dimers during the formation of photosystem II supercomplexes
physiological function
additional information
the CtpB protease is organized as a dimeric ring with the catalytic site burried within a tunnel. The PDZ domain controls access to the protease tunnel. Residues Ser309, Lys334, and Gln338 function as catalytic triad mediating cleavage of the 4FA substrate. A peptide ligand, which copurifies and cocrystallizes with CtpB, is observed at the entrance of the protease tunnel near the catalytic triad
physiological function
-
stromal processing peptidase is essential for chloroplast biogenesis at the early growth stage and for rice root development
physiological function
-
PrC plays a protective role in oxidative stress in Clonostachys rosea. PrC is required for protection against stress-induced inhibition of conidial germination in the presence of nematode cuticle and plays a role in scavenging reactive oxygen species by oxidants and heat shock
physiological function
spore formation in Bacillus subtilis relies on a regulated intramembrane proteolysis pathway, involving the enzyme, that synchronizes mother-cell and forespore development. Activating protease CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation. Activation of the SpoIV RIP pathway is induced by the concerted activity of enzyme CtpB and a second signaling protease, SpoIVB. Molecular basis of this SpoIV transmembrane signaling, the enzyme resembles a minimal version of a self-compartmentalizing protease regulated by a unique allosteric mechanism, overview
physiological function
-
Lack of protease Prc suppresses bile sensitivity in Dam-, Wec-, PhoP-, DamX-, and SeqA- mutants of Salmonella enterica, and increases bile resistance in the wild type. Changes in the activity of penicillin binding proteins PBP3, PBP4, PBP5/6 and PBP7 are detected in a Prc- background, suggesting that peptidoglycan remodeling might contribute to bile resistance
physiological function
heterologous expression in the 4E-3 mutant strain of the model non-nitrogen-fixing cyanobacterium Synechocystis sp. PCC 6803, which lacks any psbA gene. The resultant strain cannot grow photoautotrophically. These Synechocystis 6803 cells are incapable of PSII-mediated oxygen evolution. This D1 isoform, sentinel D1, represents a class of D1 protein that, when incorporated in a PSII complex, ensures that PSII cannot mediate water oxidation, thus allowing oxygen-sensitive processes such as nitrogen fixation to occur in cyanobacterial cells
physiological function
-
disruption of the ctpA gene leads to decreased heat tolerance and increased sensitivity when exposed to components of the host immune system. The ctpA mutant strain is attenuated for virulence in a murine model of infection
physiological function
-
protease Prc is involved in virulence. Mutation of Prc also results in susceptibility to multiple environmental stresses, including H2O2, sodium dodecylsulfate, and osmolarity stresses. The amounts of 34 periplasmic proteins are lower in the Prc mutant than in wild-type. These proteins are associated with proteolysis, biosynthesis of macromolecules, carbohydrate or energy metabolism, signal transduction, and protein translocation or folding. Prc stabilizes and directly binds to dipeptidyl peptidase DppP which contributes to full virulence
physiological function
a mutant lacking CtpA retains all D1 protein in precursor form, confirming that CtpA is solely responsible for processing. A knockout Ctpa mutant is lethal under normal growth conditions but is viable with sucrose under low-light conditions. Viable plants show deficiencies in PSII and thylakoid stacking. The mutant retains both monomer and dimer forms of the PSII complexes that, although nonfunctional, contain both the core and extrinsic subunits. This mutant is also essentially devoid of PSII supercomplexes. A knock-down mutant expressing about 2% wild-type level of CtpA shows normal growth under low light but is stunted and accumulats D1 protein precursor under high light
physiological function
photosystem II core protein D1 is inserted into the thylakoid membrane with a C-terminal extension which requires cleavage by C-terminal processing protease CtpA, to allow subsequent assembly of the oxygen-evolving complex. D1 precursor insertion as well as its conversion to mature D1 under various light conditions is seen only in the thylakoid membrane
physiological function
-
the enzyme is essential for photosystem II assembly
physiological function
-
the enzyme supports virulence by working in complex with the outer membrane lipoprotein LbcA to degrade cell wall hydrolases
physiological function
-
PrC plays a protective role in oxidative stress in Clonostachys rosea. PrC is required for protection against stress-induced inhibition of conidial germination in the presence of nematode cuticle and plays a role in scavenging reactive oxygen species by oxidants and heat shock
-
physiological function
-
Lack of protease Prc suppresses bile sensitivity in Dam-, Wec-, PhoP-, DamX-, and SeqA- mutants of Salmonella enterica, and increases bile resistance in the wild type. Changes in the activity of penicillin binding proteins PBP3, PBP4, PBP5/6 and PBP7 are detected in a Prc- background, suggesting that peptidoglycan remodeling might contribute to bile resistance
-
Show AA Sequence and Transmembrane Helices (3552 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
45000
75000
75000 - 80000
-
the enzyme possesses an N-terminal domain, a PDZ domain and a C-terminal catalytic domain
78500
-
TspH6, enzyme protein with six additional His residues at the C-terminus, sedimentation equilibrium
75000
-
TspH6, enzyme protein with six additional His residues at the C-terminus, calculation from sequence of cDNA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
the CtpB protease is organized as a dimeric ring with the catalytic site burried within a tunnel, domain organization of CtpB, overview
hexamer
monomer
monomer
1 * 50000, recombinant enzyme, SDS-PAGE and light scattering
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
contains an transit peptide of 142 amino acids, precursor is proteolytically inactive
proteolytic modification
-
the enzyme contains both, a transit peptide and a signal sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, all CtpB crystals are grown at 19°C using sitting-drop vapor-diffusion method, X-ray diffraction structure determination and crystal structure analysis
mutant enzyme DELTAN37, sitting drop vapor diffusion method, using 0.1 M sodium acetate, pH 4.0, and 0.6 M ammonium dihydrogen phosphate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D369A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
D441A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
D441N
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
D505A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
E433A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
E449A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
G375A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
G376A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H19A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H203A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H34A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H553A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
H60A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
K455A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
K455R
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
R371A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
R444A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S372A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S428A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S430A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S430C
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
S432A
hydrolysis of the 105 variant of N-terminal domain of lambda repressor
T452A
no hydrolysis of the 105 variant of N-terminal domain of lambda repressor
V229E
-
increased Km for 2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
V229Q
-
increased Km for 2N-[[(1-sulfono-5-naphthyl)amino]ethyl]aminosuccinyl-Ala-Ala-Arg-Ala-Ala-[Nepsilon-[4-[4-(dimethylamino)phenylazo]benzoyl]lysyl]-(6-aminocaproyl)2-Glu-Asn-Tyr-Ala-Leu-Ala-Ala
E97Q
no enzymic activity, but binding of transit peptide is not disturbed
H94L
no enzymic activity, but binding of transit peptide is not disturbed
D149A
-
very little protein detectable, processing of D1 protein of photosystem II takes place
D376A
-
very little protein detectable, processing of D1 protein of photosystem II takes place
R198A
-
very little protein detectable, processing of D1 protein of photosystem II takes place
V205M/G282C
mutations mimic Prochlorococcus marinus D1 protein in mutant background accumulating divinyl chlorophyll. Energy transfer in CP47 is interrupted in photosystem II containing divinyl chlorophylls. The V205M/G282C mutation does not recover the energy transfer pathway in CP47, instead, the mutation allows the excitation energy transfer from CP43 to CP47, which neighbors in the photosystem II dimer
additional information
additional information
O48870
downregulation of the enzyme by antisense technique in transgenic plants results in many lines with lethal seedlings
additional information
the enzyme-deficient strain 1330DELTActpa is generated by allelic exchange, the mutant produces smaller colonies on enriched agar plates and exhibits a 50% decrease in growth rate in enriched liquid medium and no growth in salt-free enriched medium, the mutant cells show a spherical shape, increased cell diameter, and membranes partially dissociated from the cell envelope compared to the wild-type cells, smooth phenotype, overview, the virulence of the wild-type strain 1330 is reduced by the mutant strain 1330DELTAcptA in murine spleen, overview
additional information
-
deletion of N-terminal amino acids 206-660, and deletion of C-terminal amino acids 1-334, both peptides are efficiently labelled by a competitive inhibitor of the enzyme marked with photoaffinity lable
additional information
the [1-874] deletion mutant lacking the C-terminus is inactive
additional information
-
the Glu945 deletion mutant shows leaf chlorosis at the early seedling stage but inhibition of root growth during the whole growth period
additional information
-
deletion of enzyme gene, no processing of D1 protein of photosystem II, no photoautotrophic growth of cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
treatment with more than 0.15% v/v Triton X-100 results in loss of enzyme activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, prolonged storage, proteolytic cleavage into two fragments of 50000 and 25000 Da
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from leaves by anion exchange chromatography, hydroxyapatite chromatography, and gel filtration, refolded recombinant His-tagged CtpA by nickel affinity chromatography with a poor yield of active enzyme
partially purified from spinach, recombinant protein from Escherichia coli using His-tag
-
recombinant His-tagged enzyme from Escherichia coli strains BL21(DE3)pLysS or B834(DE3) by nickel affinity chromatography and gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
creation of non functional mutants by insertional mutagenesis, strains carrying the mutation are growth deficient, and more sensitive to desiccation and detergents than the wild type strain
-
expressed in Escherichia coli BL21(DE3) cells
expression in the non-nitrogen-fixing cyanobacterium Synechocystis sp. PCC 6803
expression of the His-tagged enzyme in Escherichia coli strains BL21(DE3)pLysS or B834(DE3)
gene ctpA, DNA and amino acid sequence determination and analysis, genomic organization and structure, complementation of the mutant strain 1330DELTActpa by expression of wild-type gene ctpA
gene ctpA, expression of His-tagged CtpA in Escherichia coli mainly in inclusion bodies
gene prc from three strains, DNA and amino acid sequence determination and analysis, prc is located in a gene cluster encoding an extreme stress response system composed of anti-sigma factor MucA, negative regulator MucB, and ECF alternative sigma factor AlgU, regulation, overview
-
ORFs SLL2008 and SLL2009 encoding the C- and N-terminal enzyme part, respectively, operon organization
-
overexpressed in Arabidopsis thaliana, expressed as His-tag fusion protein in Escherichia coli
-
sequence analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the ctpA gene encoding C-terminal processing protease is maximal upon exposure to conditions encountered during infection
-
hyperosmotic shock (0.5-1.5 M NaCl) and treatment with cadmium (0.01-0.1 mM) and lead (0.02-0.2 mM) do not affect the expression of prC
isoform cPsbA4 is exclusively expressed during nighttime
the mRNA expression of prC is up-regulated by oxidants (0.5 mM of H2O2 and 5 mM of menadione achieve a maximal effect after 20 min) and heat shock (maximal effect after 20 min at 33-37C), most likely through the stress response element
hyperosmotic shock (0.5-1.5 M NaCl) and treatment with cadmium (0.01-0.1 mM) and lead (0.02-0.2 mM) do not affect the expression of prC
-
hyperosmotic shock (0.5-1.5 M NaCl) and treatment with cadmium (0.01-0.1 mM) and lead (0.02-0.2 mM) do not affect the expression of prC
-
-
the mRNA expression of prC is up-regulated by oxidants (0.5 mM of H2O2 and 5 mM of menadione achieve a maximal effect after 20 min) and heat shock (maximal effect after 20 min at 33-37C), most likely through the stress response element
-
the mRNA expression of prC is up-regulated by oxidants (0.5 mM of H2O2 and 5 mM of menadione achieve a maximal effect after 20 min) and heat shock (maximal effect after 20 min at 33-37C), most likely through the stress response element
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
solubilization from inclusion bodies and refolding of recombinant His-tagged CtpA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
drug development
the enzyme is a target for development of herbicides
agriculture
the enzyme is a target for general broad-spectrum herbicides
agriculture
-
potential target for the discovery of a general broad-spectrum herbicide
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Keiler, K.C.; Sauer, R.T.
Tsp protease
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
460-461
1998
Escherichia coli, Bacillus subtilis, Bartonella bacilliformis, Haemophilus influenzae, Neisseria gonorrhoeae
-
brenda
Beebe, K.D.; Shin, J.N.; Peng, J.; Chaudhury, C.; Khera, J.; Pei, D.H.
Substrate recognition through a PDZ domain in tail-specific protease
Biochemistry
39
3149-3155
2000
Escherichia coli
brenda
Liao, D.I.; Qian, J.; Chisholm, D.A.; Jordan, D.B.; Diner, B.A.
Crystal structures of the photosystem II D1 C-terminal processing protease
Nat. Struct. Biol.
7
749-753
2000
Tetradesmus obliquus
brenda
Keiler, K.C.; Sauer, R.T.
Sequence determinants of C-terminal substrate recognition by the Tsp protease
J. Biol. Chem.
271
2589-2593
1996
Escherichia coli
brenda
Keiler, K.C.; Silber, K.R.; Downard, K.M.; Papayannopoulos, I.A.; Biemann, K.; Sauer, R.T.
C-terminal specific protein degradation: activity and substrate specificity of the Tsp protease
Protein Sci.
4
1507-1515
1995
Escherichia coli
brenda
Keiler, K.C.; Sauer, R.T.
Identification of active site residues of the Tsp protease
J. Biol. Chem.
270
28864-28868
1995
Escherichia coli (P23865)
brenda
Silber, K.R.; Keiler, K.C.; Sauer, R.T.
Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini
Proc. Natl. Acad. Sci. USA
89
295-299
1992
Escherichia coli
brenda
Shestakov, S.V.; Anbudurai, P.R.; Stanbekova, G.E.; Gadzhiev, A.; Lind, L.K.; Pakrasi, H.B.
Molecular cloning and characterization of the ctpA gene encoding a carboxy-terminal processing protease. Analysis of a spontanous photosystem II-deficient mutant strain of the cyanobacterium Synechocystis sp. PCC 6803
J. Biol. Chem.
269
19354-19359
1994
Synechocystis sp.
brenda
Inagaki, N.; Yamamoto, Y.; Mori, H.; Satoh, K.
Carboxy-terminal processing protease for the D1 precursor protein: cloning and sequencing of the spinach cDNA
Plant Mol. Biol.
30
39-50
1996
Spinacia oleracea
brenda
Inagaki, N.; Maitra, R.; Satoh, K.; Pakrasi, H.B.
Amino acid residues that are critical for in vivo catalytic activity of CtpA, the carboxyl-terminus processing protease for the D1 protein of photosystem II
J. Biol. Chem.
276
30099-30105
2001
Synechocystis sp.
brenda
Yamamoto, Y.; Inagaki, N.; Satoh, K.
Overexpression and characterization of carboxyl-terminal processing protease for precursor D1 protein: regulation of enzyme-substrate interaction by molecular environments
J. Biol. Chem.
276
7518-7525
2001
Spinacia oleracea
brenda
Trost, J.T.; Chisholm, D.A.; Jordan, D.B.; Diner, B.A.
The D1 C-terminal processing protease of photosystem II from Scenedesmus obliquus. Protein purification and gene characterization in wild type and processing mutants
J. Biol. Chem.
272
20348-20356
1997
Tetradesmus obliquus
brenda
Bowyeer, J.R.; Packer, J.C.L.; McCormack, B.A.; Whitelegge, J.P.; Robinson, C.; Taylor, M.A.
Carboxyl-terminal processing of the D1 protein and photoactivation of water-splitting photosystem II. Partial purification and characterization of the processing enzyme from Scendesmus obliquus and Pisum sativum
J. Biol. Chem.
267
5424-5433
1992
Lathyrus oleraceus, Tetradesmus obliquus
brenda
Yamamoto, Y.; Satoh, K.
Competitive inhibition analysis of the enzyme-substrate interaction in the carboxy-terminal processing of the precursor D1 protein of photosystem II reaction center using substituted oligopeptides
FEBS Lett.
430
261-265
1998
Spinacia oleracea
brenda
Taguchi, F.; Yamamoto, Y.; Satoh, K.
Recognition of the structure around the site of cleavage by the carboxyl-terminal processing protease for D1 precursor protein of the photosystem II reaction center
J. Biol. Chem.
270
10711-10716
1995
Spinacia oleracea
brenda
Chaal, B.K.; Mould, R.M.; Barbrook, A.C.; Grays, J.C.; Howe, C.J.
Characterization of a cDNA encoding the thylakoid processing peptidase from Arabidopsis thaliana. Implications for the origin and catalytic mechanism of the enzyme
J. Biol. Chem.
273
689-692
1998
Arabidopsis thaliana
brenda
Spetea, C.; Hundal, T.; Lohmann, F.; Andersson, B.
GTP bound to chloroplast thylakoid membranes is required for light-induced, multienzyme degradation of the photosystem II D1 protein
Proc. Natl. Acad. Sci. USA
96
6547-6552
1999
Spinacia oleracea
brenda
Kanervo, E.; Spetea, C.; Nishiyama, Y.; Murata, N.; Andersson, B.; Aro, E.M.
Dissecting a cyanobacterial proteolytic system: efficiency in inducing degradation of the D1 protein of photosystem II in cyanobacteria and plants
Biochim. Biophys. Acta
1607
131-140
2003
Synechocystis sp.
brenda
Spetea, C.; Keren, N.; Hundal, T.; Doan, J.M.; Ohad, I.; Andersson, B.
GTP enhances the degradation of the photosystem II D1 protein irrespective of its conformational heterogeneity at the Q(B) site
J. Biol. Chem.
275
7205-7211
2000
Lathyrus oleraceus, Spinacia oleracea
brenda
Richter, S.; Lamppa, G.K.
Structural properties of the chloroplast stromal processing peptidase required for its function in transit peptide removal
J. Biol. Chem.
278
39497-39502
2003
Lathyrus oleraceus (Q40983)
brenda
Chaal, B.K.; Ishida, K.i.; Green, B.R.
A thylakoidal processing peptidase from the heterokont alga Heterosigma akashiwo
Plant Mol. Biol.
52
463-472
2003
Heterosigma akashiwo
brenda
Ivleva, N.B.; Shestakov, S.V.; Pakrasi, H.B.
The carboxyl-terminal extension of the precursor D1 protein of photosystem II is required for optimal photosynthetic performance of the cyanobacterium Synechocystis sp. PCC 6803
Plant Physiol.
124
1403-1412
2000
Synechocystis sp.
brenda
Bandara, A.B.; Sriranganathan, N.; Schurig, G.G.; Boyle, S.M.
Carboxyl-terminal protease regulates Brucella suis morphology in culture and persistence in macrophages and mice
J. Bacteriol.
187
5767-5775
2005
Brucella suis bv. 1 (A0A0H3G8P9)
brenda
Tadokoro, A.; Hayashi, H.; Kishimoto, T.; Makino, Y.; Fujisaki, S.; Nishimura, Y.
Interaction of the Escherichia coli lipoprotein NlpI with periplasmic Prc (Tsp) protease
J. Biochem.
135
185-191
2004
Escherichia coli
brenda
Reiling, S.A.; Jansen, J.A.; Henley, B.J.; Singh, S.; Chattin, C.; Chandler, M.; Rowen, D.W.
Prc protease promotes mucoidy in mucA mutants of Pseudomonas aeruginosa
Microbiology
151
2251-2261
2005
Pseudomonas aeruginosa
brenda
Fabbri, B.J.; Duff, S.M.G.; Remsen, E.E.; Chen, Y.C.S.; Anderson, J.C.; CaJacob, C.A.
The carboxyterminal processing protease of D1 protein: Expression, purification and enzymology of the recombinant and native spinach proteins
Pest Manag. Sci.
61
682-690
2005
Spinacia oleracea (Q41376), Spinacia oleracea
brenda
Richter, S.; Zhong, R.; Lamppa, G.
Function of the stromal processing peptidase in the chloroplast import pathway
Physiol. Plant.
123
362-368
2005
Anabaena sp., Arabidopsis thaliana (O48870), Chlamydomonas reinhardtii, Lathyrus oleraceus (Q40983), Lotus japonicus, Medicago truncatula, Oryza sativa, Plasmodium falciparum (Q8MVZ1), Synechocystis sp.
-
brenda
Gilbert, K.B.; Vanderlinde, E.M.; Yost, C.K.
Mutagenesis of the carboxy terminal protease CtpA decreases desiccation tolerance in Rhizobium leguminosarum
FEMS Microbiol. Lett.
272
65-74
2007
Rhizobium leguminosarum
brenda
Duff, S.M.; Chen, Y.S.; Fabbri, B.J.; Yalamanchili, G.; Hamper, B.C.; Walker, D.M.; Brookfield, F.A.; Boyd, E.A.; Ashton, M.R.; Yarnold, C.J.; CaJacob, C.A.
The carboxyterminal processing protease of D1 protein: herbicidal activity of novel inhibitors of the recombinant and native spinach enzymes
Pestic. Biochem. Physiol.
88
1-13
2007
Spinacia oleracea
-
brenda
Booij-James, I.S.; Edelman, M.; Mattoo, A.K.
Nitric oxide donor-mediated inhibition of phosphorylation shows that light-mediated degradation of photosystem II D1 protein and phosphorylation are not tightly linked
Planta
229
1347-1352
2009
Landoltia punctata
brenda
Hoge, R.; Laschinski, M.; Jaeger, K.E.; Wilhelm, S.; Rosenau, F.
The subcellular localization of a C-terminal processing protease in Pseudomonas aeruginosa
FEMS Microbiol. Lett.
316
23-30
2011
Pseudomonas aeruginosa
brenda
Zhang, W.; Li, H.; Li, W.; Yang, Y.; Feng, L.; Liu, Y.; Qi, C.
Screening for inhibitors of plant protease D1 using novel monoclonal antibodies directed against its carboxyl terminal
Hybridoma
30
223-227
2011
Spinacia oleracea
brenda
Yue, R.; Wang, X.; Chen, J.; Ma, X.; Zhang, H.; Mao, C.; Wu, P.
A rice stromal processing peptidase regulates chloroplast and root development
Plant Cell Physiol.
51
475-485
2010
Oryza sativa Indica Group
brenda
Zou, C.G.; Xu, Y.F.; Liu, W.J.; Zhou, W.; Tao, N.; Tu, H.H.; Huang, X.W.; Yang, J.K.; Zhang, K.Q.
Expression of a serine protease gene prC is up-regulated by oxidative stress in the fungus Clonostachys rosea: implications for fungal survival
PLoS ONE
5
e13386
2010
Clonostachys rosea, Clonostachys rosea 611
brenda
Yokono, M.; Tomo, T.; Nagao, R.; Ito, H.; Tanaka, A.; Akimoto, S.
Alterations in photosynthetic pigments and amino acid composition of D1 protein change energy distribution in photosystem II
Biochim. Biophys. Acta
1817
754-759
2012
Synechocystis sp. (Q55669), Synechocystis sp.
brenda
Mastny, M.; Heuck, A.; Kurzbauer, R.; Heiduk, A.; Boisguerin, P.; Volkmer, R.; Ehrmann, M.; Rodrigues, C.D.; Rudner, D.Z.; Clausen, T.
CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in Bacillus subtilis
Cell
155
647-658
2013
Bacillus subtilis (O35002)
brenda
Hernandez, S.B.; Ayala, J.A.; Rico-Perez, G.; Garcia-del Portillo, F.; Casadesus, J.
Increased bile resistance in Salmonella enterica mutants lacking Prc periplasmic protease
Int. Microbiol.
16
87-92
2013
Salmonella enterica, Salmonella enterica SL1344
brenda
Sugiura, M.; Ogami, S.; Kusumi, M.; Un, S.; Rappaport, F.; Boussac, A.
Environment of TyrZ in photosystem II from Thermosynechococcus elongatus in which PsbA2 is the D1 protein
J. Biol. Chem.
287
13336-13347
2012
Thermosynechococcus vestitus (P0A446)
brenda
Wegener, K.M.; Nagarajan, A.; Pakrasi, H.B.
An atypical psbA gene encodes a sentinel D1 protein to form a physiologically relevant inactive photosystem II complex in cyanobacteria
J. Biol. Chem.
290
3764-3774
2015
Crocosphaera subtropica ATCC 51142 (B1WZS6)
brenda
Carroll, R.; Rivera, F.; Cavaco, C.; Johnson, G.; Martin, D.; Shaw, L.
The lone S41 family C-terminal processing protease in Staphylococcus aureus is localized to the cell wall and contributes to virulence
Microbiology
160
1737-1748
2014
Staphylococcus aureus
brenda
Deng, C.Y.; Deng, A.H.; Sun, S.T.; Wang, L.; Wu, J.; Wu, Y.; Chen, X.Y.; Fang, R.X.; Wen, T.Y.; Qian, W.
The periplasmic PDZ domain-containing protein Prc modulates full virulence, envelops stress responses, and directly interacts with dipeptidyl peptidase of Xanthomonas oryzae pv. oryzae
Mol. Plant Microbe Interact.
27
101-112
2014
Xanthomonas oryzae pv. oryzae
brenda
Che, Y.; Fu, A.; Hou, X.; McDonald, K.; Buchanan, B.B.; Huang, W.; Luan, S.
C-terminal processing of reaction center protein D1 is essential for the function and assembly of photosystem II in Arabidopsis
Proc. Natl. Acad. Sci. USA
110
16247-16252
2013
Arabidopsis thaliana (O23614)
brenda
Selao, T.T.; Zhang, L.; Knoppova, J.; Komenda, J.; Norling, B.
Photosystem II Assembly Steps Take Place in the Thylakoid Membrane of the Cyanobacterium Synechocystis sp. PCC6803
Plant Cell Physiol.
57
95-104
2016
Synechocystis sp. PCC 6803 (Q55669)
brenda
Shi, Y.; Che, Y.; Wang, Y.; Luan, S.; Hou, X.
Loss of mature D1 leads to compromised CP43 assembly in Arabidopsis thaliana
BMC Plant Biol.
21
106
2021
Arabidopsis thaliana
brenda
Chueh, C.K.; Som, N.; Ke, L.C.; Ho, M.R.; Reddy, M.; Chang, C.I.
Structural basis for the differential regulatory roles of the PDZ domain in C-terminal processing proteases
mBio
10
e01129-19
2019
Arabidopsis thaliana
brenda
Hsu, H.C.; Wang, M.; Kovach, A.; Darwin, A.J.; Li, H.
Pseudomonas aeruginosa C-terminal processing protease CtpA assembles into a hexameric structure that requires activation by a spiral-shaped lipoprotein-binding partner
mBio
13
e0368021
2022
Pseudomonas aeruginosa
brenda
EXTERNAL LINKS (specific for EC-Number 3.4.21.102)
Transporter Classification Database (TCDB): 9.B.174.1.2, 9.B.174.1.1
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
