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Information on EC 3.4.21.102 - C-terminal processing peptidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9FIH8

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.102 C-terminal processing peptidase
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9FIH8 not found.
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chloroplast processing enzyme
O48870
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stromal processing peptidase
O48870
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C-terminal processing peptidase
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C-terminal processing protease
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carboxy terminal-processing proteinase
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carboxyl-terminal-processing peptidase 2
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chloroplast protein precursor processing proteinase
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CtpA gene product
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D1 preprotein-processing proteinase
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D1 protein-processing enzyme
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photosystem D1 protein precursor carboxyl-terminal processing protease
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photosystem II D1 C-terminal processing protease
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photosystem II D1 protein
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photosystem II D1 protein processing proteinase
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PRC protein
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processing peptidase
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protease Re
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proteinase CtpA
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proteinase, chloroplast protein precursor-processing
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stromal processing peptidase
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tail-specific protease
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thylakoid protein precursor processing peptidase
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Tsp protease
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additional information
O48870
the enzyme probably belongs to the M16 peptidase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
reaction mechanism, process model, substrate recognition, overview
O48870
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
216484-75-2
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92480-11-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D1 polypeptide of photosystem II + H2O
?
show the reaction diagram
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-
?
D1 protein precursor + H2O
mature D1 protein + ?
show the reaction diagram
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-
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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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
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
O48870
the enzyme contains a HXXEH zinc-binding motif
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
chloroplast thylakoid lumen
Manually annotated by BRENDA team
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integral membrane protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37900
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calculation from sequnce of cDNA
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
O48870
downregulation of the enzyme by antisense technique in transgenic plants results in many lines with lethal seedlings
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
single gene, sequence analysis, expression analysis
O48870
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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, Lotus japonicus, Medicago truncatula, Oryza sativa, Pisum sativum (Q40983), Plasmodium falciparum (Q8MVZ1), Synechocystis sp.
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team