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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
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
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
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
-
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
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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
-
-
-
?
Ac-WARAAARAAARBAAB + H2O
?
-
i.e. peptide BAS9
-
-
?
Ac-WARAAARAAARBGGB + H2O
?
-
i.e. peptide BAS10
-
-
?
anti-sigma factor MucA + H2O
?
Arc repressor + H2O
?
-
C-terminal sequence: GRIGA, endoproteolyric cleavage
-
-
?
C-terminal 19 amino acids of preD1 protein + H2O
pre-peptide of D1 + oligomer of 11 amino acids
-
replacement of Ala at the cleaving site by Gly, Val, Pro reduces the rate of proteolysis to 50, 30 and 0% of the control
-
?
Cab1R protein precursor + H2O
?
-
-
-
-
?
Cab2R protein precursor + H2O
?
-
-
-
-
?
core protein S1 precursor + H2O
?
-
-
-
?
cytochrome-b562-WVAAA + H2O
?
-
cytochrome b562 with a C-terminal attachment, fast hydrolysis
-
-
?
cytochrome-b562-WVAAK + H2O
?
-
cytochrome b562 with a C-terminal attachment, no hydrolysis
-
-
?
cytochrome-b562-WVAAV + H2O
?
-
cytochrome b562 with a C-terminal attachment, slow hydrolysis
-
-
?
cytochrome-b562-WVAGA + H2O
?
-
cytochrome b562 with a C-terminal attachment, slow hydrolysis
-
-
?
cytochrome-b562-WVAYA + H2O
?
-
cytochrome b562 with a C-terminal attachment, fast hydrolysis
-
-
?
cytochrome-b562-WVLAA + H2O
?
-
cytochrome b562 with a C-terminal attachment, fast hydrolysis
-
-
?
cytochrome-b562-WVQAA + H2O
?
-
cytochrome b562 with a C-terminal attachment, slow hydrolysis
-
-
?
D1 polypeptide of photosystem II + H2O
?
D1 protein precursor + H2O
mature D1 protein + ?
-
-
-
?
maize preOEC17
OEC17 + presequence
-
precursor of thylakoid lumen protein OEC17
-
?
membrane protein SpoIVFA + H2O
?
P-24 peptide + H2O
?
peptide substrate comprising the 24 C-terminal residues of spinach pre-D1 protein
-
-
?
pre-D1 protein + H2O
D1 protein + peptide
-
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
-
-
?
pre-LHCP protein + H2O
LHCP protein + transit peptide
-
-
-
?
pre-RBCS protein + H2O
RBCS protein + transit peptide
-
-
-
-
?
prePsbO + H2O
PsbO + presequence
-
precursor of thylakoid lumen protein PsbO or OEC33
-
?
ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit precursor + H2O
?
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
variant of the lambda repressor + H2O
?
additional information
?
-
anti-sigma factor MucA + H2O
?
-
-
-
-
?
anti-sigma factor MucA + H2O
?
-
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
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
enzymatic cleavage occurs on the C-terminal site of Ala344
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
investigation of substrate recognition sites
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
determination of the catalytic important residues
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
removal of the C-terminal extension
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
removal of the C-terminal extension
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
in vivo proteolytic processing of pre-D1, no other protease can compensate for its loss
-
-
?
D1 protein + H2O
?
C-terminal processing of D1 protein
-
-
?
D1 protein + H2O
?
substrate from spinach
-
-
?
F-24 peptide + H2O
?
-
peptide substrate comprising the 24 C-terminal residues of spinach pre-D1 protein, N-terminally fluorescence-labeled with a fluorescein isothiocyanate group
-
-
?
F-24 peptide + H2O
?
peptide substrate comprising the 24 C-terminal residues of spinach pre-D1 protein, N-terminally fluorescence-labeled with a fluorescein isothiocyanate group
-
-
?
membrane protein SpoIVFA + H2O
?
-
-
-
?
membrane protein SpoIVFA + H2O
?
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
-
-
?
NIpI protein + H2O
?
-
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
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-
?
NIpI protein + H2O
?
-
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
-
-
?
Protein + H2O
?
-
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
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-
?
Protein + H2O
?
-
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.
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-
?
Protein + H2O
?
-
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
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-
?
Protein + H2O
?
-
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.
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
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
-
-
?
Protein + H2O
?
-
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.
-
-
?
Protein + H2O
?
-
Tsp is a component of the ssrA RNA protein-tagging pathway for the removal of incorrectly synthesized proteins
-
-
?
Protein + H2O
?
-
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
-
-
?
Protein + H2O
?
-
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.
-
-
?
Protein + H2O
?
-
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
-
-
?
Protein + H2O
?
-
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.
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
SP-4 peptide + H2O
?
-
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
-
-
?
SP-4 peptide + H2O
?
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
-
-
?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
variant of the lambda repressor + H2O
?
-
C-terminal sequence: WVAAA, endoproteolytic cleavage
-
-
?
variant of the lambda repressor + H2O
?
C-terminal sequence: WVAAA, endoproteolytic cleavage
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
substrate recognition by specific protein-protein interaction, endoprotease activity, overview
-
-
?
additional information
?
-
O48870
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
-
-
?
additional information
?
-
O48870
substrate recognition by specific protein-protein interaction, endoprotease activity, overview
-
-
?
additional information
?
-
the enzyme belongs to the family of endoproteases involved in the maturation of proteins destined for the cell envelope
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
substrate recognition by specific protein-protein interaction, endoprotease activity, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
substrate recognition by specific protein-protein interaction, endoprotease activity, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
substrate recognition by specific protein-protein interaction, endoprotease activity, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
substrate recognition by specific protein-protein interaction, endoprotease activity, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
substrate recognition by specific protein-protein interaction, endoprotease activity, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
substrate recognition by specific protein-protein interaction, endoprotease activity, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
substrate recognition by specific protein-protein interaction, endoprotease activity, overview
-
-
?
additional information
?
-
Thermosynechococcus vestitus
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
anti-sigma factor MucA + H2O
?
-
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
-
-
?
Cab1R protein precursor + H2O
?
-
-
-
-
?
Cab2R protein precursor + H2O
?
-
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
D1 protein + H2O
?
C-terminal processing of D1 protein
-
-
?
membrane protein SpoIVFA + H2O
?
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
-
-
?
NIpI protein + H2O
?
-
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
-
-
?
pre-D1 protein + H2O
D1 protein + peptide
-
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
-
-
?
pre-LHCP protein + H2O
LHCP protein + transit peptide
-
-
-
?
pre-RBCS protein + H2O
RBCS protein + transit peptide
-
-
-
-
?
ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit precursor + H2O
?
-
-
-
-
?
additional information
?
-
D1 polypeptide of photosystem II + H2O
?
-
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
-
-
-
?
D1 polypeptide of photosystem II + H2O
?
-
in vivo proteolytic processing of pre-D1, no other protease can compensate for its loss
-
-
?
Protein + H2O
?
-
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.
-
-
?
Protein + H2O
?
-
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.
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
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.
-
-
?
Protein + H2O
?
-
Tsp is a component of the ssrA RNA protein-tagging pathway for the removal of incorrectly synthesized proteins
-
-
?
Protein + H2O
?
-
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.
-
-
?
Protein + H2O
?
-
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.
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
O48870
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
-
-
?
additional information
?
-
the enzyme belongs to the family of endoproteases involved in the maturation of proteins destined for the cell envelope
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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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
D253A
-
no processing of D1 protein of photosystem II
D376A
-
very little protein detectable, processing of D1 protein of photosystem II takes place
E316A
-
no processing of D1 protein of photosystem II
E316Q
-
no photoautotrophic growth of cells
K338A
-
no processing of D1 protein of photosystem II
K338H
-
no photoautotrophic growth of cells
K338R
-
no photoautotrophic growth of cells
R198A
-
very little protein detectable, processing of D1 protein of photosystem II takes place
R255A
-
no processing of D1 protein of photosystem II
R255H
-
no photoautotrophic growth of cells
S313A
-
no processing of D1 protein of photosystem II
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
L132M/L210M
-
crystallization data of selenomethionyl derivative
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 Glu945 deletion mutant shows leaf chlorosis at the early seedling stage but inhibition of root growth during the whole growth period
additional information
the [1-874] deletion mutant lacking the C-terminus is inactive
additional information
-
deletion of enzyme gene, no processing of D1 protein of photosystem II, no photoautotrophic growth of cells
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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
Bacillus subtilis, Bartonella bacilliformis, Escherichia coli, 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
Pisum sativum, 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
Pisum sativum, 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
Pisum sativum (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., Synechocystis sp., Chlamydomonas reinhardtii, Lotus japonicus, Medicago truncatula, Oryza sativa, Arabidopsis thaliana (O48870), Pisum sativum (Q40983), Plasmodium falciparum (Q8MVZ1)
-
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